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Volumn 114, Issue , 2015, Pages 134-146

N-terminal protein modifications: Bringing back into play the ribosome

Author keywords

Co translational modifications; Methionine aminopeptidase; N myristoyltransferase; N terminal; N acetyltransferase; Peptide deformylase

Indexed keywords

ACYLTRANSFERASE; METALLOPROTEINASE; METHIONYL AMINOPEPTIDASE; PEPTIDE DEFORMYLASE; POLYPEPTIDE; PROTEIN N MYRISTOYLTRANSFERASE; UBIQUITIN; AMIDASE;

EID: 84930649538     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2014.11.008     Document Type: Review
Times cited : (134)

References (176)
  • 2
    • 34247281027 scopus 로고    scopus 로고
    • Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence
    • U. Raue, S. Oellerer, and S. Rospert Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence J. Biol. Chem. 282 2007 7809 7816
    • (2007) J. Biol. Chem. , vol.282 , pp. 7809-7816
    • Raue, U.1    Oellerer, S.2    Rospert, S.3
  • 3
    • 66849109240 scopus 로고    scopus 로고
    • The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
    • G. Kramer, D. Boehringer, N. Ban, and B. Bukau The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins Nat. Struct. Mol. Biol. 16 2009 589 597
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 589-597
    • Kramer, G.1    Boehringer, D.2    Ban, N.3    Bukau, B.4
  • 4
    • 0020570527 scopus 로고
    • Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles
    • M. Kozak Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles Microbiol. Rev. 47 1983 1 45
    • (1983) Microbiol. Rev. , vol.47 , pp. 1-45
    • Kozak, M.1
  • 5
    • 79953721157 scopus 로고    scopus 로고
    • Translation initiation: variations in the mechanism can be anticipated
    • N. Malys, and J.E. McCarthy Translation initiation: variations in the mechanism can be anticipated Cell. Mol. Life Sci. 68 2011 991 1003
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 991-1003
    • Malys, N.1    McCarthy, J.E.2
  • 6
    • 0026778267 scopus 로고
    • Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli
    • J.M. Guillon, Y. Mechulam, J.M. Schmitter, S. Blanquet, and G. Fayat Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli J. Bacteriol. 174 1992 4294 4301
    • (1992) J. Bacteriol. , vol.174 , pp. 4294-4301
    • Guillon, J.M.1    Mechulam, Y.2    Schmitter, J.M.3    Blanquet, S.4    Fayat, G.5
  • 8
    • 0029959716 scopus 로고    scopus 로고
    • Molecular recognition governing the initiation of translation in Escherichia coli. A review
    • E. Schmitt, J.M. Guillon, T. Meinnel, Y. Mechulam, F. Dardel, and S. Blanquet Molecular recognition governing the initiation of translation in Escherichia coli. A review Biochimie 78 1996 543 554
    • (1996) Biochimie , vol.78 , pp. 543-554
    • Schmitt, E.1    Guillon, J.M.2    Meinnel, T.3    Mechulam, Y.4    Dardel, F.5    Blanquet, S.6
  • 9
    • 0027488750 scopus 로고
    • Two acidic residues of Escherichia coli methionyl-tRNA synthetase act as negative discriminants towards the binding of non-cognate tRNA anticodons
    • E. Schmitt, T. Meinnel, M. Panvert, Y. Mechulam, and S. Blanquet Two acidic residues of Escherichia coli methionyl-tRNA synthetase act as negative discriminants towards the binding of non-cognate tRNA anticodons J. Mol. Biol. 233 1993 615 628
    • (1993) J. Mol. Biol. , vol.233 , pp. 615-628
    • Schmitt, E.1    Meinnel, T.2    Panvert, M.3    Mechulam, Y.4    Blanquet, S.5
  • 10
    • 40549132858 scopus 로고    scopus 로고
    • Tools for analyzing and predicting N-terminal protein modifications
    • T. Meinnel, and C. Giglione Tools for analyzing and predicting N-terminal protein modifications Proteomics 8 2008 626 649
    • (2008) Proteomics , vol.8 , pp. 626-649
    • Meinnel, T.1    Giglione, C.2
  • 12
    • 63449111532 scopus 로고    scopus 로고
    • Chapter 6 Mass spectrometric characterization of the thirteen subunits of bovine respiratory complexes that are encoded in mitochondrial DNA
    • J.E. Walker, J. Carroll, M.C. Altman, and I.M. Fearnley Chapter 6 Mass spectrometric characterization of the thirteen subunits of bovine respiratory complexes that are encoded in mitochondrial DNA Methods Enzymol. 456 2009 111 131
    • (2009) Methods Enzymol. , vol.456 , pp. 111-131
    • Walker, J.E.1    Carroll, J.2    Altman, M.C.3    Fearnley, I.M.4
  • 13
    • 0031021278 scopus 로고    scopus 로고
    • The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides
    • M. Unseld, J.R. Marienfeld, and A. Brennicke The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides Nat. Genet. 15 1997 57 61
    • (1997) Nat. Genet. , vol.15 , pp. 57-61
    • Unseld, M.1    Marienfeld, J.R.2    Brennicke, A.3
  • 14
  • 15
    • 0035543404 scopus 로고    scopus 로고
    • Organellar peptide deformylases: universality of the N-terminal methionine cleavage mechanism
    • C. Giglione, and T. Meinnel Organellar peptide deformylases: universality of the N-terminal methionine cleavage mechanism Trends Plant Sci. 6 2001 566 572
    • (2001) Trends Plant Sci. , vol.6 , pp. 566-572
    • Giglione, C.1    Meinnel, T.2
  • 17
    • 80052377663 scopus 로고    scopus 로고
    • Non-coding nucleotides and amino acids near the active site regulate peptide deformylase expression and inhibitor susceptibility in Chlamydia trachomatis
    • X. Bao, N.D. Pachikara, C.B. Oey, A. Balakrishnan, L.F. Westblade, M. Tan, T. Chase Jr., B.E. Nickels, and H. Fan Non-coding nucleotides and amino acids near the active site regulate peptide deformylase expression and inhibitor susceptibility in Chlamydia trachomatis Microbiology 157 2011 2569 2581
    • (2011) Microbiology , vol.157 , pp. 2569-2581
    • Bao, X.1    Pachikara, N.D.2    Oey, C.B.3    Balakrishnan, A.4    Westblade, L.F.5    Tan, M.6    Chase, T.7    Nickels, B.E.8    Fan, H.9
  • 18
    • 84901393468 scopus 로고    scopus 로고
    • Redox regulation of methionine aminopeptidase 2 activity
    • J. Chiu, J.W. Wong, and P.J. Hogg Redox regulation of methionine aminopeptidase 2 activity J. Biol. Chem. 289 2014 15035 15043
    • (2014) J. Biol. Chem. , vol.289 , pp. 15035-15043
    • Chiu, J.1    Wong, J.W.2    Hogg, P.J.3
  • 19
    • 61449192364 scopus 로고    scopus 로고
    • Identification of iron-responsive proteins expressed by Chlamydia trachomatis reticulate bodies during intracellular growth
    • B.D. Dill, S. Dessus-Babus, and J.E. Raulston Identification of iron-responsive proteins expressed by Chlamydia trachomatis reticulate bodies during intracellular growth Microbiology 155 2009 210 219
    • (2009) Microbiology , vol.155 , pp. 210-219
    • Dill, B.D.1    Dessus-Babus, S.2    Raulston, J.E.3
  • 20
    • 0036616943 scopus 로고    scopus 로고
    • Toxoplasma gondii asexual development: identification of developmentally regulated genes and distinct patterns of gene expression
    • M.D. Cleary, U. Singh, I.J. Blader, J.L. Brewer, and J.C. Boothroyd Toxoplasma gondii asexual development: identification of developmentally regulated genes and distinct patterns of gene expression Eukaryot. Cell. 1 2002 329 340
    • (2002) Eukaryot. Cell. , vol.1 , pp. 329-340
    • Cleary, M.D.1    Singh, U.2    Blader, I.J.3    Brewer, J.L.4    Boothroyd, J.C.5
  • 21
    • 27544493101 scopus 로고    scopus 로고
    • Cerebrospinal fluid proteomic analysis reveals dysregulation of methionine aminopeptidase-2 expression in human and mouse neurofibromatosis 1-associated glioma
    • B. Dasgupta, Y. Yi, B. Hegedus, J.D. Weber, and D.H. Gutmann Cerebrospinal fluid proteomic analysis reveals dysregulation of methionine aminopeptidase-2 expression in human and mouse neurofibromatosis 1-associated glioma Cancer Res. 65 2005 9843 9850
    • (2005) Cancer Res. , vol.65 , pp. 9843-9850
    • Dasgupta, B.1    Yi, Y.2    Hegedus, B.3    Weber, J.D.4    Gutmann, D.H.5
  • 23
  • 24
    • 0023754392 scopus 로고
    • Cotranslational processing and protein turnover in eukaryotic cells
    • S.M. Arfin, and R.A. Bradshaw Cotranslational processing and protein turnover in eukaryotic cells Biochemistry 27 1988 7979 7984
    • (1988) Biochemistry , vol.27 , pp. 7979-7984
    • Arfin, S.M.1    Bradshaw, R.A.2
  • 25
    • 0037413729 scopus 로고    scopus 로고
    • Control of protein life-span by N-terminal methionine excision
    • C. Giglione, O. Vallon, and T. Meinnel Control of protein life-span by N-terminal methionine excision EMBO J. 22 2003 13 23
    • (2003) EMBO J. , vol.22 , pp. 13-23
    • Giglione, C.1    Vallon, O.2    Meinnel, T.3
  • 26
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • A. Varshavsky The N-end rule pathway and regulation by proteolysis Protein Sci. 20 2011 1298 1345
    • (2011) Protein Sci. , vol.20 , pp. 1298-1345
    • Varshavsky, A.1
  • 27
    • 84908478523 scopus 로고    scopus 로고
    • The eukaryotic N-end rule pathway: conserved mechanisms and diverse functions
    • D.J. Gibbs, J. Bacardit, A. Bachmair, and M.J. Holdsworth The eukaryotic N-end rule pathway: conserved mechanisms and diverse functions Trends Cell Biol. 24 2014 603 611
    • (2014) Trends Cell Biol. , vol.24 , pp. 603-611
    • Gibbs, D.J.1    Bacardit, J.2    Bachmair, A.3    Holdsworth, M.J.4
  • 28
    • 77149120798 scopus 로고    scopus 로고
    • N-terminal acetylation of cellular proteins creates specific degradation signals
    • C.S. Hwang, A. Shemorry, and A. Varshavsky N-terminal acetylation of cellular proteins creates specific degradation signals Science 327 2010 973 977
    • (2010) Science , vol.327 , pp. 973-977
    • Hwang, C.S.1    Shemorry, A.2    Varshavsky, A.3
  • 29
    • 84878195272 scopus 로고    scopus 로고
    • Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway
    • A. Shemorry, C.S. Hwang, and A. Varshavsky Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway Mol. Cell 50 2013 540 551
    • (2013) Mol. Cell , vol.50 , pp. 540-551
    • Shemorry, A.1    Hwang, C.S.2    Varshavsky, A.3
  • 30
    • 84892802083 scopus 로고    scopus 로고
    • The N-terminal methionine of cellular proteins as a degradation signal
    • H.K. Kim, R.R. Kim, J.H. Oh, H. Cho, A. Varshavsky, and C.S. Hwang The N-terminal methionine of cellular proteins as a degradation signal Cell 156 2014 158 169
    • (2014) Cell , vol.156 , pp. 158-169
    • Kim, H.K.1    Kim, R.R.2    Oh, J.H.3    Cho, H.4    Varshavsky, A.5    Hwang, C.S.6
  • 32
    • 0028053015 scopus 로고
    • Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation
    • D. Mazel, S. Pochet, and P. Marliere Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation EMBO J. 13 1994 914 923
    • (1994) EMBO J. , vol.13 , pp. 914-923
    • Mazel, D.1    Pochet, S.2    Marliere, P.3
  • 33
    • 0027971916 scopus 로고
    • Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase
    • T. Meinnel, and S. Blanquet Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase J. Bacteriol. 176 1994 7387 7390
    • (1994) J. Bacteriol. , vol.176 , pp. 7387-7390
    • Meinnel, T.1    Blanquet, S.2
  • 34
    • 0034818097 scopus 로고    scopus 로고
    • Eukaryotic peptide deformylases. Nuclear-encoded and chloroplast- targeted enzymes in Arabidopsis
    • L.M. Dirk, M.A. Williams, and R.L. Houtz Eukaryotic peptide deformylases. Nuclear-encoded and chloroplast- targeted enzymes in Arabidopsis Plant Physiol. 127 2001 97 107
    • (2001) Plant Physiol. , vol.127 , pp. 97-107
    • Dirk, L.M.1    Williams, M.A.2    Houtz, R.L.3
  • 35
    • 0035824874 scopus 로고    scopus 로고
    • Distinctive features of the two classes of eukaryotic peptide deformylases
    • A. Serero, C. Giglione, and T. Meinnel Distinctive features of the two classes of eukaryotic peptide deformylases J. Mol. Biol. 314 2001 695 708
    • (2001) J. Mol. Biol. , vol.314 , pp. 695-708
    • Serero, A.1    Giglione, C.2    Meinnel, T.3
  • 37
    • 0032540979 scopus 로고    scopus 로고
    • Control of peptide deformylase activity by metal cations
    • S. Ragusa, S. Blanquet, and T. Meinnel Control of peptide deformylase activity by metal cations J. Mol. Biol. 280 1998 515 523
    • (1998) J. Mol. Biol. , vol.280 , pp. 515-523
    • Ragusa, S.1    Blanquet, S.2    Meinnel, T.3
  • 38
    • 0033936704 scopus 로고    scopus 로고
    • Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents
    • C. Giglione, M. Pierre, and T. Meinnel Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents Mol. Microbiol. 36 2000 1197 1205
    • (2000) Mol. Microbiol. , vol.36 , pp. 1197-1205
    • Giglione, C.1    Pierre, M.2    Meinnel, T.3
  • 40
    • 0034329475 scopus 로고    scopus 로고
    • Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
    • C. Giglione, A. Serero, M. Pierre, B. Boisson, and T. Meinnel Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms EMBO J. 19 2000 5916 5929
    • (2000) EMBO J. , vol.19 , pp. 5916-5929
    • Giglione, C.1    Serero, A.2    Pierre, M.3    Boisson, B.4    Meinnel, T.5
  • 42
    • 0142152459 scopus 로고    scopus 로고
    • Genome sequences of two closely related Vibrio parahaemolyticus phages, VP16T and VP16C
    • V. Seguritan, I.W. Feng, F. Rohwer, M. Swift, and A.M. Segall Genome sequences of two closely related Vibrio parahaemolyticus phages, VP16T and VP16C J. Bacteriol. 185 2003 6434 6447
    • (2003) J. Bacteriol. , vol.185 , pp. 6434-6447
    • Seguritan, V.1    Feng, I.W.2    Rohwer, F.3    Swift, M.4    Segall, A.M.5
  • 45
    • 0036077847 scopus 로고    scopus 로고
    • The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents
    • J.P. Guilloteau, M. Mathieu, C. Giglione, V. Blanc, A. Dupuy, M. Chevrier, P. Gil, A. Famechon, T. Meinnel, and V. Mikol The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents J. Mol. Biol. 320 2002 951 962
    • (2002) J. Mol. Biol. , vol.320 , pp. 951-962
    • Guilloteau, J.P.1    Mathieu, M.2    Giglione, C.3    Blanc, V.4    Dupuy, A.5    Chevrier, M.6    Gil, P.7    Famechon, A.8    Meinnel, T.9    Mikol, V.10
  • 46
    • 0347993051 scopus 로고    scopus 로고
    • An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway
    • A. Serero, C. Giglione, A. Sardini, J. Martinez Sanz, and T. Meinnel An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway J. Biol. Chem. 278 2003 52953 52963
    • (2003) J. Biol. Chem. , vol.278 , pp. 52953-52963
    • Serero, A.1    Giglione, C.2    Sardini, A.3    Martinez Sanz, J.4    Meinnel, T.5
  • 47
    • 29644433002 scopus 로고    scopus 로고
    • The crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms
    • S. Fieulaine, C. Juillan-Binard, A. Serero, F. Dardel, C. Giglione, T. Meinnel, and J.L. Ferrer The crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms J. Biol. Chem. 280 2005 42315 42324
    • (2005) J. Biol. Chem. , vol.280 , pp. 42315-42324
    • Fieulaine, S.1    Juillan-Binard, C.2    Serero, A.3    Dardel, F.4    Giglione, C.5    Meinnel, T.6    Ferrer, J.L.7
  • 48
    • 84894139821 scopus 로고    scopus 로고
    • Understanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart
    • S. Fieulaine, M. Desmadril, T. Meinnel, and C. Giglione Understanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart Acta Crystallogr. D Biol. Crystallogr. 70 2014 242 252
    • (2014) Acta Crystallogr. D Biol. Crystallogr. , vol.70 , pp. 242-252
    • Fieulaine, S.1    Desmadril, M.2    Meinnel, T.3    Giglione, C.4
  • 49
    • 68249107043 scopus 로고    scopus 로고
    • Cotranslational processing mechanisms: towards a dynamic 3D model
    • C. Giglione, S. Fieulaine, and T. Meinnel Cotranslational processing mechanisms: towards a dynamic 3D model Trends Biochem. Sci. 34 2009 417 426
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 417-426
    • Giglione, C.1    Fieulaine, S.2    Meinnel, T.3
  • 50
    • 0034177339 scopus 로고    scopus 로고
    • Peptide deformylase of eukaryotic protists: a target for new antiparasitic agents?
    • T. Meinnel Peptide deformylase of eukaryotic protists: a target for new antiparasitic agents? Parasitol. Today 16 2000 165 168
    • (2000) Parasitol. Today , vol.16 , pp. 165-168
    • Meinnel, T.1
  • 51
    • 0033919993 scopus 로고    scopus 로고
    • Peptide deformylase in Staphylococcus aureus: resistance to inhibition is mediated by mutations in the formyltransferase gene
    • P.S. Margolis, C.J. Hackbarth, D.C. Young, W. Wang, D. Chen, Z. Yuan, R. White, and J. Trias Peptide deformylase in Staphylococcus aureus: resistance to inhibition is mediated by mutations in the formyltransferase gene Antimicrob. Agents Chemother. 44 2000 1825 1831
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 1825-1831
    • Margolis, P.S.1    Hackbarth, C.J.2    Young, D.C.3    Wang, W.4    Chen, D.5    Yuan, Z.6    White, R.7    Trias, J.8
  • 54
    • 0034916353 scopus 로고    scopus 로고
    • YkrB is the main peptide deformylase in Bacillus subtilis, a eubacterium containing two functional peptide deformylases
    • M. Haas, D. Beyer, R. Gahlmann, and C. Freiberg YkrB is the main peptide deformylase in Bacillus subtilis, a eubacterium containing two functional peptide deformylases Microbiology 147 2001 1783 1791
    • (2001) Microbiology , vol.147 , pp. 1783-1791
    • Haas, M.1    Beyer, D.2    Gahlmann, R.3    Freiberg, C.4
  • 55
    • 36949033891 scopus 로고    scopus 로고
    • Characterization of peptide deformylase2 from B. cereus
    • J.K. Park, K.H. Kim, J.H. Moon, and E.E. Kim Characterization of peptide deformylase2 from B. cereus J. Biochem. Mol. Biol. 40 2007 1050 1057
    • (2007) J. Biochem. Mol. Biol. , vol.40 , pp. 1050-1057
    • Park, J.K.1    Kim, K.H.2    Moon, J.H.3    Kim, E.E.4
  • 56
    • 0036882401 scopus 로고    scopus 로고
    • Metalloaminopeptidases: common functional themes in disparate structural surroundings
    • W.T. Lowther, and B.W. Matthews Metalloaminopeptidases: common functional themes in disparate structural surroundings Chem. Rev. 102 2002 4581 4608
    • (2002) Chem. Rev. , vol.102 , pp. 4581-4608
    • Lowther, W.T.1    Matthews, B.W.2
  • 57
    • 19044396327 scopus 로고    scopus 로고
    • Functional and developmental impact of cytosolic protein N-terminal methionine excision in Arabidopsis
    • S. Ross, C. Giglione, M. Pierre, C. Espagne, and T. Meinnel Functional and developmental impact of cytosolic protein N-terminal methionine excision in Arabidopsis Plant Physiol. 137 2005 623 637
    • (2005) Plant Physiol. , vol.137 , pp. 623-637
    • Ross, S.1    Giglione, C.2    Pierre, M.3    Espagne, C.4    Meinnel, T.5
  • 58
    • 0034144404 scopus 로고    scopus 로고
    • MAPs and POEP of the roads from prokaryotic to eukaryotic kingdoms
    • B. Datta MAPs and POEP of the roads from prokaryotic to eukaryotic kingdoms Biochimie 82 2000 95 107
    • (2000) Biochimie , vol.82 , pp. 95-107
    • Datta, B.1
  • 59
    • 72049124267 scopus 로고    scopus 로고
    • Targeting the role of N-terminal methionine processing enzymes in Mycobacterium tuberculosis
    • O.A. Olaleye, W.R. Bishai, and J.O. Liu Targeting the role of N-terminal methionine processing enzymes in Mycobacterium tuberculosis Tuberculosis 89 Suppl. 1 2009 S55 S59
    • (2009) Tuberculosis , vol.89 , pp. S55-S59
    • Olaleye, O.A.1    Bishai, W.R.2    Liu, J.O.3
  • 60
    • 0027273988 scopus 로고
    • Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme
    • S.L. Roderick, and B.W. Matthews Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme Biochemistry 32 1993 3907 3912
    • (1993) Biochemistry , vol.32 , pp. 3907-3912
    • Roderick, S.L.1    Matthews, B.W.2
  • 61
    • 18544383303 scopus 로고    scopus 로고
    • Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome
    • A. Addlagatta, M.L. Quillin, O. Omotoso, J.O. Liu, and B.W. Matthews Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome Biochemistry 44 2005 7166 7174
    • (2005) Biochemistry , vol.44 , pp. 7166-7174
    • Addlagatta, A.1    Quillin, M.L.2    Omotoso, O.3    Liu, J.O.4    Matthews, B.W.5
  • 62
    • 79959830296 scopus 로고    scopus 로고
    • Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity
    • P. Kanudia, M. Mittal, S. Kumaran, and P.K. Chakraborti Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity BMC Biochem. 12 2011 35
    • (2011) BMC Biochem. , vol.12 , pp. 35
    • Kanudia, P.1    Mittal, M.2    Kumaran, S.3    Chakraborti, P.K.4
  • 63
    • 0036235240 scopus 로고    scopus 로고
    • Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo
    • J.A. Vetro, and Y.H. Chang Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo J. Cell. Biochem. 85 2002 678 688
    • (2002) J. Cell. Biochem. , vol.85 , pp. 678-688
    • Vetro, J.A.1    Chang, Y.H.2
  • 64
    • 84885083813 scopus 로고    scopus 로고
    • Discovery of a new genetic variant of methionine aminopeptidase from Streptococci with possible post-translational modifications: biochemical and structural characterization
    • T. Arya, C. Kishor, V. Saddanapu, R. Reddi, and A. Addlagatta Discovery of a new genetic variant of methionine aminopeptidase from Streptococci with possible post-translational modifications: biochemical and structural characterization PLoS One 8 2013 e75207
    • (2013) PLoS One , vol.8
    • Arya, T.1    Kishor, C.2    Saddanapu, V.3    Reddi, R.4    Addlagatta, A.5
  • 65
    • 0032515029 scopus 로고    scopus 로고
    • Structure of human methionine aminopeptidase-2 complexed with fumagillin
    • S. Liu, J. Widom, C.W. Kemp, and J. Clardy Structure of human methionine aminopeptidase-2 complexed with fumagillin Science 282 1998 1324 1327
    • (1998) Science , vol.282 , pp. 1324-1327
    • Liu, S.1    Widom, J.2    Kemp, C.W.3    Clardy, J.4
  • 68
    • 0030567984 scopus 로고    scopus 로고
    • Evidence that the human homologue of a rat initiation factor-2 associated protein (p67) is a methionine aminopeptidase
    • X. Li, and Y.H. Chang Evidence that the human homologue of a rat initiation factor-2 associated protein (p67) is a methionine aminopeptidase Biochem. Biophys. Res. Commun. 227 1996 152 159
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 152-159
    • Li, X.1    Chang, Y.H.2
  • 69
    • 0035213737 scopus 로고    scopus 로고
    • Protection of translation initiation factor eIF2 phosphorylation correlates with eIF2-associated glycoprotein p67 levels and requires the lysine-rich domain I of p67
    • R. Datta, P. Choudhury, M. Bhattacharya, F. Soto Leon, Y. Zhou, and B. Datta Protection of translation initiation factor eIF2 phosphorylation correlates with eIF2-associated glycoprotein p67 levels and requires the lysine-rich domain I of p67 Biochimie 83 2001 919 931
    • (2001) Biochimie , vol.83 , pp. 919-931
    • Datta, R.1    Choudhury, P.2    Bhattacharya, M.3    Soto Leon, F.4    Zhou, Y.5    Datta, B.6
  • 70
    • 0037442848 scopus 로고    scopus 로고
    • Negative regulation of the protection of eIF2alpha phosphorylation activity by a unique acidic domain present at the N-terminus of p67
    • R. Datta, R. Tammali, and B. Datta Negative regulation of the protection of eIF2alpha phosphorylation activity by a unique acidic domain present at the N-terminus of p67 Exp. Cell. Res. 283 2003 237 246
    • (2003) Exp. Cell. Res. , vol.283 , pp. 237-246
    • Datta, R.1    Tammali, R.2    Datta, B.3
  • 71
    • 33746826546 scopus 로고    scopus 로고
    • The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2alpha from phosphorylation by kinases
    • B. Datta, R. Datta, A. Ghosh, and A. Majumdar The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2alpha from phosphorylation by kinases Arch. Biochem. Biophys. 452 2006 138 148
    • (2006) Arch. Biochem. Biophys. , vol.452 , pp. 138-148
    • Datta, B.1    Datta, R.2    Ghosh, A.3    Majumdar, A.4
  • 73
    • 34548260523 scopus 로고    scopus 로고
    • The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions
    • E. Kowalinski, G. Bange, B. Bradatsch, E. Hurt, K. Wild, and I. Sinning The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions FEBS Lett. 581 2007 4450 4454
    • (2007) FEBS Lett. , vol.581 , pp. 4450-4454
    • Kowalinski, E.1    Bange, G.2    Bradatsch, B.3    Hurt, E.4    Wild, K.5    Sinning, I.6
  • 74
    • 33646164893 scopus 로고    scopus 로고
    • Ebp1 is a dsRNA-binding protein associated with ribosomes that modulates eIF2alpha phosphorylation
    • M. Squatrito, M. Mancino, L. Sala, and G.F. Draetta Ebp1 is a dsRNA-binding protein associated with ribosomes that modulates eIF2alpha phosphorylation Biochem. Biophys. Res. Commun. 344 2006 859 868
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 859-868
    • Squatrito, M.1    Mancino, M.2    Sala, L.3    Draetta, G.F.4
  • 75
    • 84870820752 scopus 로고    scopus 로고
    • Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to the 60S ribosomal subunit
    • B.J. Greber, D. Boehringer, C. Montellese, and N. Ban Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to the 60S ribosomal subunit Nat. Struct. Mol. Biol. 19 2012 1228 1233
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1228-1233
    • Greber, B.J.1    Boehringer, D.2    Montellese, C.3    Ban, N.4
  • 77
    • 33646582609 scopus 로고    scopus 로고
    • Nuclear recycling of the pre-60S ribosomal subunit-associated factor Arx1 depends on Rei1 in Saccharomyces cerevisiae
    • N.J. Hung, and A.W. Johnson Nuclear recycling of the pre-60S ribosomal subunit-associated factor Arx1 depends on Rei1 in Saccharomyces cerevisiae Mol. Cell. Biol. 26 2006 3718 3727
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3718-3727
    • Hung, N.J.1    Johnson, A.W.2
  • 81
    • 80053415277 scopus 로고    scopus 로고
    • Protein alpha-N-acetylation studied by N-terminomics
    • P. Van Damme, T. Arnesen, and K. Gevaert Protein alpha-N-acetylation studied by N-terminomics FEBS J. 278 2011 3822 3834
    • (2011) FEBS J. , vol.278 , pp. 3822-3834
    • Van Damme, P.1    Arnesen, T.2    Gevaert, K.3
  • 83
    • 84859515208 scopus 로고    scopus 로고
    • Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features
    • M111 015131
    • W.V. Bienvenut, D. Sumpton, A. Martinez, S. Lilla, C. Espagne, T. Meinnel, and C. Giglione Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features Mol. Cell. Proteomics 11 2012 M111 015131
    • (2012) Mol. Cell. Proteomics , vol.11
    • Bienvenut, W.V.1    Sumpton, D.2    Martinez, A.3    Lilla, S.4    Espagne, C.5    Meinnel, T.6    Giglione, C.7
  • 84
    • 33744971921 scopus 로고    scopus 로고
    • Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex
    • T. Arnesen, D. Gromyko, F. Pendino, A. Ryningen, J.E. Varhaug, and J.R. Lillehaug Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex Oncogene 25 2006 4350 4360
    • (2006) Oncogene , vol.25 , pp. 4350-4360
    • Arnesen, T.1    Gromyko, D.2    Pendino, F.3    Ryningen, A.4    Varhaug, J.E.5    Lillehaug, J.R.6
  • 85
    • 67650085001 scopus 로고    scopus 로고
    • Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization
    • K.K. Starheim, D. Gromyko, R. Evjenth, A. Ryningen, J.E. Varhaug, J.R. Lillehaug, and T. Arnesen Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization Mol. Cell. Biol. 29 2009 3569 3581
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3569-3581
    • Starheim, K.K.1    Gromyko, D.2    Evjenth, R.3    Ryningen, A.4    Varhaug, J.E.5    Lillehaug, J.R.6    Arnesen, T.7
  • 86
    • 77955297697 scopus 로고    scopus 로고
    • Depletion of the human Nalpha-terminal acetyltransferase A induces p53-dependent apoptosis and p53-independent growth inhibition
    • D. Gromyko, T. Arnesen, A. Ryningen, J.E. Varhaug, and J.R. Lillehaug Depletion of the human Nalpha-terminal acetyltransferase A induces p53-dependent apoptosis and p53-independent growth inhibition Int. J. Cancer 127 2010 2777 2789
    • (2010) Int. J. Cancer , vol.127 , pp. 2777-2789
    • Gromyko, D.1    Arnesen, T.2    Ryningen, A.3    Varhaug, J.E.4    Lillehaug, J.R.5
  • 88
    • 33845293454 scopus 로고    scopus 로고
    • Human arrest defective 1 acetylates and activates beta-catenin, promoting lung cancer cell proliferation
    • J.H. Lim, J.W. Park, and Y.S. Chun Human arrest defective 1 acetylates and activates beta-catenin, promoting lung cancer cell proliferation Cancer Res. 66 2006 10677 10682
    • (2006) Cancer Res. , vol.66 , pp. 10677-10682
    • Lim, J.H.1    Park, J.W.2    Chun, Y.S.3
  • 89
    • 70450218735 scopus 로고    scopus 로고
    • Correlation of expression of human arrest-defective-1 (hARD1) protein with breast cancer
    • M. Yu, M. Ma, C. Huang, H. Yang, J. Lai, S. Yan, L. Li, M. Xiang, and D. Tan Correlation of expression of human arrest-defective-1 (hARD1) protein with breast cancer Cancer Invest. 27 2009 978 983
    • (2009) Cancer Invest. , vol.27 , pp. 978-983
    • Yu, M.1    Ma, M.2    Huang, C.3    Yang, H.4    Lai, J.5    Yan, S.6    Li, L.7    Xiang, M.8    Tan, D.9
  • 92
    • 80555131132 scopus 로고    scopus 로고
    • N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex
    • D.C. Scott, J.K. Monda, E.J. Bennett, J.W. Harper, and B.A. Schulman N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex Science 334 2011 674 678
    • (2011) Science , vol.334 , pp. 674-678
    • Scott, D.C.1    Monda, J.K.2    Bennett, E.J.3    Harper, J.W.4    Schulman, B.A.5
  • 93
    • 79958027934 scopus 로고    scopus 로고
    • N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum
    • G.M. Forte, M.R. Pool, and C.J. Stirling N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum PLoS Biol. 9 2011 e1001073
    • (2011) PLoS Biol. , vol.9
    • Forte, G.M.1    Pool, M.R.2    Stirling, C.J.3
  • 95
    • 84904458790 scopus 로고    scopus 로고
    • Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding
    • W.M. Holmes, B.K. Mannakee, R.N. Gutenkunst, and T.R. Serio Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding Nat. Commun. 5 2014 4383
    • (2014) Nat. Commun. , vol.5 , pp. 4383
    • Holmes, W.M.1    Mannakee, B.K.2    Gutenkunst, R.N.3    Serio, T.R.4
  • 96
    • 84859490749 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases: when the start matters
    • K.K. Starheim, K. Gevaert, and T. Arnesen Protein N-terminal acetyltransferases: when the start matters Trends Biochem. Sci. 37 2012 152 161
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 152-161
    • Starheim, K.K.1    Gevaert, K.2    Arnesen, T.3
  • 97
    • 84872613178 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases in cancer
    • T.V. Kalvik, and T. Arnesen Protein N-terminal acetyltransferases in cancer Oncogene 32 2013 269 276
    • (2013) Oncogene , vol.32 , pp. 269-276
    • Kalvik, T.V.1    Arnesen, T.2
  • 98
    • 79955761504 scopus 로고    scopus 로고
    • Proteome-derived peptide libraries allow detailed analysis of the substrate specificities of N(alpha)-acetyltransferases and point to hNaa10p as the post-translational actin N(alpha)-acetyltransferase
    • M110 004580
    • P. Van Damme, R. Evjenth, H. Foyn, K. Demeyer, P.J. De Bock, J.R. Lillehaug, J. Vandekerckhove, T. Arnesen, and K. Gevaert Proteome-derived peptide libraries allow detailed analysis of the substrate specificities of N(alpha)-acetyltransferases and point to hNaa10p as the post-translational actin N(alpha)-acetyltransferase Mol. Cell. Proteomics 10 2011 M110 004580
    • (2011) Mol. Cell. Proteomics , vol.10
    • Van Damme, P.1    Evjenth, R.2    Foyn, H.3    Demeyer, K.4    De Bock, P.J.5    Lillehaug, J.R.6    Vandekerckhove, J.7    Arnesen, T.8    Gevaert, K.9
  • 99
    • 34250001423 scopus 로고    scopus 로고
    • An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus
    • D.T. Mackay, C.H. Botting, G.L. Taylor, and M.F. White An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus Mol. Microbiol. 64 2007 1540 1548
    • (2007) Mol. Microbiol. , vol.64 , pp. 1540-1548
    • Mackay, D.T.1    Botting, C.H.2    Taylor, G.L.3    White, M.F.4
  • 100
    • 84883342432 scopus 로고    scopus 로고
    • Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog
    • G. Liszczak, and R. Marmorstein Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog Proc. Natl. Acad. Sci. U. S. A. 110 2013 14652 14657
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 14652-14657
    • Liszczak, G.1    Marmorstein, R.2
  • 104
    • 84878701862 scopus 로고    scopus 로고
    • Potential involvement of N-terminal acetylation in the quantitative regulation of the epsilon subunit of chloroplast ATP synthase under drought stress
    • S. Hoshiyasu, K. Kohzuma, K. Yoshida, M. Fujiwara, Y. Fukao, A. Yokota, and K. Akashi Potential involvement of N-terminal acetylation in the quantitative regulation of the epsilon subunit of chloroplast ATP synthase under drought stress Biosci. Biotechnol. Biochem. 77 2013 998 1007
    • (2013) Biosci. Biotechnol. Biochem. , vol.77 , pp. 998-1007
    • Hoshiyasu, S.1    Kohzuma, K.2    Yoshida, K.3    Fujiwara, M.4    Fukao, Y.5    Yokota, A.6    Akashi, K.7
  • 106
    • 80054694313 scopus 로고    scopus 로고
    • Structure of a Ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation
    • G. Liszczak, T. Arnesen, and R. Marmorstein Structure of a Ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation J. Biol. Chem. 286 2011 37002 37010
    • (2011) J. Biol. Chem. , vol.286 , pp. 37002-37010
    • Liszczak, G.1    Arnesen, T.2    Marmorstein, R.3
  • 107
    • 52949119208 scopus 로고    scopus 로고
    • Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for N(alpha)-acetylation of ribosomal protein S18
    • M.W. Vetting, D.C. Bareich, M. Yu, and J.S. Blanchard Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for N(alpha)-acetylation of ribosomal protein S18 Protein Sci. 17 2008 1781 1790
    • (2008) Protein Sci. , vol.17 , pp. 1781-1790
    • Vetting, M.W.1    Bareich, D.C.2    Yu, M.3    Blanchard, J.S.4
  • 108
    • 20444445924 scopus 로고    scopus 로고
    • A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium
    • M.W. Vetting, L.P. de Carvalho, S.L. Roderick, and J.S. Blanchard A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium J. Biol. Chem. 280 2005 22108 22114
    • (2005) J. Biol. Chem. , vol.280 , pp. 22108-22114
    • Vetting, M.W.1    De Carvalho, L.P.2    Roderick, S.L.3    Blanchard, J.S.4
  • 110
    • 0017389254 scopus 로고
    • Protein modification enzymes associated with the protein-synthesizing complex from rabbit reticulocytes. Protein kinase, phosphoprotein phosphatase, and acetyltransferase
    • J.A. Traugh, and S.B. Sharp Protein modification enzymes associated with the protein-synthesizing complex from rabbit reticulocytes. Protein kinase, phosphoprotein phosphatase, and acetyltransferase J. Biol. Chem. 252 1977 3738 3744
    • (1977) J. Biol. Chem. , vol.252 , pp. 3738-3744
    • Traugh, J.A.1    Sharp, S.B.2
  • 111
    • 38649122076 scopus 로고    scopus 로고
    • Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes
    • B. Polevoda, S. Brown, T.S. Cardillo, S. Rigby, and F. Sherman Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes J. Cell. Biochem. 103 2008 492 508
    • (2008) J. Cell. Biochem. , vol.103 , pp. 492-508
    • Polevoda, B.1    Brown, S.2    Cardillo, T.S.3    Rigby, S.4    Sherman, F.5
  • 112
    • 79961232419 scopus 로고    scopus 로고
    • Bioinformatics analysis of a Saccharomyces cerevisiae N-terminal proteome provides evidence of alternative translation initiation and post-translational N-terminal acetylation
    • K. Helsens, P. Van Damme, S. Degroeve, L. Martens, T. Arnesen, J. Vandekerckhove, and K. Gevaert Bioinformatics analysis of a Saccharomyces cerevisiae N-terminal proteome provides evidence of alternative translation initiation and post-translational N-terminal acetylation J. Proteome Res. 10 2011 3578 3589
    • (2011) J. Proteome Res. , vol.10 , pp. 3578-3589
    • Helsens, K.1    Van Damme, P.2    Degroeve, S.3    Martens, L.4    Arnesen, T.5    Vandekerckhove, J.6    Gevaert, K.7
  • 113
    • 0025980490 scopus 로고
    • Rat liver polysome N alpha-acetyltransferase: substrate specificity
    • R. Yamada, and R.A. Bradshaw Rat liver polysome N alpha-acetyltransferase: substrate specificity Biochemistry 30 1991 1017 1021
    • (1991) Biochemistry , vol.30 , pp. 1017-1021
    • Yamada, R.1    Bradshaw, R.A.2
  • 114
    • 0024401730 scopus 로고
    • Purification and characterization of hen oviduct N alpha-acetyltransferase
    • K. Kamitani, K. Narita, and F. Sakiyama Purification and characterization of hen oviduct N alpha-acetyltransferase J. Biol. Chem. 264 1989 13188 13193
    • (1989) J. Biol. Chem. , vol.264 , pp. 13188-13193
    • Kamitani, K.1    Narita, K.2    Sakiyama, F.3
  • 115
  • 116
    • 0141640821 scopus 로고    scopus 로고
    • The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides
    • M. Gautschi, S. Just, A. Mun, S. Ross, P. Rucknagel, Y. Dubaquie, A. Ehrenhofer-Murray, and S. Rospert The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides Mol. Cell. Biol. 23 2003 7403 7414
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7403-7414
    • Gautschi, M.1    Just, S.2    Mun, A.3    Ross, S.4    Rucknagel, P.5    Dubaquie, Y.6    Ehrenhofer-Murray, A.7    Rospert, S.8
  • 117
    • 0016691755 scopus 로고
    • Acetylation of nascent polypeptide chains on rat liver polyribosomes in vivo and in vitro
    • A. Pestana, and H.C. Pitot Acetylation of nascent polypeptide chains on rat liver polyribosomes in vivo and in vitro Biochemistry 14 1975 1404 1412
    • (1975) Biochemistry , vol.14 , pp. 1404-1412
    • Pestana, A.1    Pitot, H.C.2
  • 118
    • 0014948880 scopus 로고
    • Role of methionine in the initiation of haemoglobin synthesis
    • R. Jackson, and T. Hunter Role of methionine in the initiation of haemoglobin synthesis Nature 227 1970 672 676
    • (1970) Nature , vol.227 , pp. 672-676
    • Jackson, R.1    Hunter, T.2
  • 119
    • 0008558313 scopus 로고
    • Ovalbumin: a secreted protein without a transient hydrophobic leader sequence
    • R.D. Palmiter, J. Gagnon, and K.A. Walsh Ovalbumin: a secreted protein without a transient hydrophobic leader sequence Proc. Natl. Acad. Sci. U. S. A. 75 1978 94 98
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 94-98
    • Palmiter, R.D.1    Gagnon, J.2    Walsh, K.A.3
  • 121
    • 0016154293 scopus 로고
    • Alteration in the acetylation level of ribosomal protein L12 during growth cycle of Escherichia coli
    • S. Ramagopal, and A.R. Subramanian Alteration in the acetylation level of ribosomal protein L12 during growth cycle of Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 71 1974 2136 2140
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 2136-2140
    • Ramagopal, S.1    Subramanian, A.R.2
  • 122
    • 0030948184 scopus 로고    scopus 로고
    • Myristoylation
    • J.A. Boutin Myristoylation Cell. Signal 9 1997 15 35
    • (1997) Cell. Signal , vol.9 , pp. 15-35
    • Boutin, J.A.1
  • 124
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristoylation
    • T.A. Farazi, G. Waksman, and J.I. Gordon The biology and enzymology of protein N-myristoylation J. Biol. Chem. 276 2001 39501 39504
    • (2001) J. Biol. Chem. , vol.276 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 126
    • 1642340046 scopus 로고    scopus 로고
    • Myristoylation of viral and bacterial proteins
    • S. Maurer-Stroh, and F. Eisenhaber Myristoylation of viral and bacterial proteins Trends Microbiol. 12 2004 178 185
    • (2004) Trends Microbiol. , vol.12 , pp. 178-185
    • Maurer-Stroh, S.1    Eisenhaber, F.2
  • 127
    • 78650516076 scopus 로고    scopus 로고
    • Post-translational myristoylation: fat matters in cellular life and death
    • D.D. Martin, E. Beauchamp, and L.G. Berthiaume Post-translational myristoylation: fat matters in cellular life and death Biochimie 93 2011 18 31
    • (2011) Biochimie , vol.93 , pp. 18-31
    • Martin, D.D.1    Beauchamp, E.2    Berthiaume, L.G.3
  • 128
    • 46849114454 scopus 로고    scopus 로고
    • Protein lipidation meets proteomics
    • T. Meinnel, and C. Giglione Protein lipidation meets proteomics Front. Biosci. 13 2008 6326 6340
    • (2008) Front. Biosci. , vol.13 , pp. 6326-6340
    • Meinnel, T.1    Giglione, C.2
  • 129
    • 84872411888 scopus 로고    scopus 로고
    • High-throughput profiling of N-myristoylation substrate specificity across species including pathogens
    • J.A. Traverso, C. Giglione, and T. Meinnel High-throughput profiling of N-myristoylation substrate specificity across species including pathogens Proteomics 13 2013 25 36
    • (2013) Proteomics , vol.13 , pp. 25-36
    • Traverso, J.A.1    Giglione, C.2    Meinnel, T.3
  • 130
    • 0036295384 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: refinement of the sequence motif and its taxon-specific differences
    • S. Maurer-Stroh, B. Eisenhaber, and F. Eisenhaber N-terminal N-myristoylation of proteins: refinement of the sequence motif and its taxon-specific differences J. Mol. Biol. 317 2002 523 540
    • (2002) J. Mol. Biol. , vol.317 , pp. 523-540
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 132
    • 2942564436 scopus 로고    scopus 로고
    • N-Terminal myristoylation predictions by ensembles of neural networks
    • G. Bologna, C. Yvon, S. Duvaud, and A.L. Veuthey N-Terminal myristoylation predictions by ensembles of neural networks Proteomics 4 2004 1626 1632
    • (2004) Proteomics , vol.4 , pp. 1626-1632
    • Bologna, G.1    Yvon, C.2    Duvaud, S.3    Veuthey, A.L.4
  • 133
    • 9144256852 scopus 로고    scopus 로고
    • Predicting N-terminal myristoylation sites in plant proteins
    • S. Podell, and M. Gribskov Predicting N-terminal myristoylation sites in plant proteins BMC Genomics 5 2004 37
    • (2004) BMC Genomics , vol.5 , pp. 37
    • Podell, S.1    Gribskov, M.2
  • 137
    • 0025834950 scopus 로고
    • Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase
    • D.A. Rudnick, C.A. McWherter, W.J. Rocque, P.J. Lennon, D.P. Getman, and J.I. Gordon Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase J. Biol. Chem. 266 1991 9732 9739
    • (1991) J. Biol. Chem. , vol.266 , pp. 9732-9739
    • Rudnick, D.A.1    McWherter, C.A.2    Rocque, W.J.3    Lennon, P.J.4    Getman, D.P.5    Gordon, J.I.6
  • 138
    • 0035822617 scopus 로고    scopus 로고
    • Pre-steady-state kinetic studies of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase mutants identify residues involved in catalysis
    • T.A. Farazi, J.K. Manchester, G. Waksman, and J.I. Gordon Pre-steady-state kinetic studies of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase mutants identify residues involved in catalysis Biochemistry 40 2001 9177 9186
    • (2001) Biochemistry , vol.40 , pp. 9177-9186
    • Farazi, T.A.1    Manchester, J.K.2    Waksman, G.3    Gordon, J.I.4
  • 139
    • 0023868823 scopus 로고
    • 11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase
    • R.O. Heuckeroth, D.A. Towler, S.P. Adams, L. Glaser, and J.I. Gordon 11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase J. Biol. Chem. 263 1988 2127 2133
    • (1988) J. Biol. Chem. , vol.263 , pp. 2127-2133
    • Heuckeroth, R.O.1    Towler, D.A.2    Adams, S.P.3    Glaser, L.4    Gordon, J.I.5
  • 141
    • 0242290313 scopus 로고    scopus 로고
    • Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote
    • B. Boisson, C. Giglione, and T. Meinnel Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote J. Biol. Chem. 278 2003 43418 43429
    • (2003) J. Biol. Chem. , vol.278 , pp. 43418-43429
    • Boisson, B.1    Giglione, C.2    Meinnel, T.3
  • 142
    • 0023109534 scopus 로고
    • Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase
    • D.A. Towler, S.R. Eubanks, D.S. Towery, S.P. Adams, and L. Glaser Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase J. Biol. Chem. 262 1987 1030 1036
    • (1987) J. Biol. Chem. , vol.262 , pp. 1030-1036
    • Towler, D.A.1    Eubanks, S.R.2    Towery, D.S.3    Adams, S.P.4    Glaser, L.5
  • 144
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • C. Wilcox, J.S. Hu, and E.N. Olson Acylation of proteins with myristic acid occurs cotranslationally Science 238 1987 1275 1278
    • (1987) Science , vol.238 , pp. 1275-1278
    • Wilcox, C.1    Hu, J.S.2    Olson, E.N.3
  • 145
    • 0030657584 scopus 로고    scopus 로고
    • Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction
    • published erratum appears in J Biol Chem 1998 Mar 6;273(10):5988
    • C.J. Glover, K.D. Hartman, and R.L. Felsted Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction published erratum appears in J Biol Chem 1998 Mar 6;273(10):5988 J. Biol. Chem. 272 1997 28680 28689
    • (1997) J. Biol. Chem. , vol.272 , pp. 28680-28689
    • Glover, C.J.1    Hartman, K.D.2    Felsted, R.L.3
  • 146
    • 0023819706 scopus 로고
    • In vitro synthesis of pp60v-src: myristylation in a cell-free system
    • I. Deichaite, L.P. Casson, H.P. Ling, and M.D. Resh In vitro synthesis of pp60v-src: myristylation in a cell-free system Mol. Cell. Biol. 8 1988 4295 4301
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4295-4301
    • Deichaite, I.1    Casson, L.P.2    Ling, H.P.3    Resh, M.D.4
  • 147
    • 78751511233 scopus 로고    scopus 로고
    • Suppression of human immunodeficiency virus type-1 production by coexpression of catalytic-region-deleted N-myristoyltransferase mutants
    • N. Takamune, T. Kuroe, N. Tanada, S. Shoji, and S. Misumi Suppression of human immunodeficiency virus type-1 production by coexpression of catalytic-region-deleted N-myristoyltransferase mutants Biological Pharm. Bull. 33 2010 2018 2023
    • (2010) Biological Pharm. Bull. , vol.33 , pp. 2018-2023
    • Takamune, N.1    Kuroe, T.2    Tanada, N.3    Shoji, S.4    Misumi, S.5
  • 148
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins
    • R.M. Peitzsch, and S. McLaughlin Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins Biochemistry 32 1993 10436 10443
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 149
    • 0032516482 scopus 로고    scopus 로고
    • Chain length and temperature dependence of the reversible association of model acylated proteins with lipid bilayers
    • C.T. Pool, and T.E. Thompson Chain length and temperature dependence of the reversible association of model acylated proteins with lipid bilayers Biochemistry 37 1998 10246 10255
    • (1998) Biochemistry , vol.37 , pp. 10246-10255
    • Pool, C.T.1    Thompson, T.E.2
  • 151
    • 84876773827 scopus 로고    scopus 로고
    • Roles of N-Terminal fatty acid acylations in membrane compartment partitioning: arabidopsis h-type thioredoxins as a case study
    • J.A. Traverso, C. Micalella, A. Martinez, S.C. Brown, B. Satiat-Jeunemaitre, T. Meinnel, and C. Giglione Roles of N-Terminal fatty acid acylations in membrane compartment partitioning: arabidopsis h-type thioredoxins as a case study Plant Cell. 25 2013 1056 1077
    • (2013) Plant Cell. , vol.25 , pp. 1056-1077
    • Traverso, J.A.1    Micalella, C.2    Martinez, A.3    Brown, S.C.4    Satiat-Jeunemaitre, B.5    Meinnel, T.6    Giglione, C.7
  • 153
    • 1342322684 scopus 로고    scopus 로고
    • Vertical-scanning mutagenesis of amino acids in a model N-myristoylation motif reveals the major amino-terminal sequence requirements for protein N-myristoylation
    • T. Utsumi, K. Nakano, T. Funakoshi, Y. Kayano, S. Nakao, N. Sakurai, H. Iwata, and R. Ishisaka Vertical-scanning mutagenesis of amino acids in a model N-myristoylation motif reveals the major amino-terminal sequence requirements for protein N-myristoylation Eur. J. Biochem. 271 2004 863 874
    • (2004) Eur. J. Biochem. , vol.271 , pp. 863-874
    • Utsumi, T.1    Nakano, K.2    Funakoshi, T.3    Kayano, Y.4    Nakao, S.5    Sakurai, N.6    Iwata, H.7    Ishisaka, R.8
  • 154
    • 0035971107 scopus 로고    scopus 로고
    • Amino acid residue penultimate to the amino-terminal gly residue strongly affects two cotranslational protein modifications, N-myristoylation and N-acetylation
    • T. Utsumi, M. Sato, K. Nakano, D. Takemura, H. Iwata, and R. Ishisaka Amino acid residue penultimate to the amino-terminal gly residue strongly affects two cotranslational protein modifications, N-myristoylation and N-acetylation J. Biol. Chem. 276 2001 10505 10513
    • (2001) J. Biol. Chem. , vol.276 , pp. 10505-10513
    • Utsumi, T.1    Sato, M.2    Nakano, K.3    Takemura, D.4    Iwata, H.5    Ishisaka, R.6
  • 156
    • 0014686198 scopus 로고
    • Kinetics of maturation of the amino termini of the cell proteins of Escherichia coli
    • M.J. Pine Kinetics of maturation of the amino termini of the cell proteins of Escherichia coli Biochim. Biophys. Acta 174 1969 359 372
    • (1969) Biochim. Biophys. Acta , vol.174 , pp. 359-372
    • Pine, M.J.1
  • 158
    • 0013999452 scopus 로고
    • Experiments on hemoglobin polypeptide chain initiation and on the shielding actionof the ribosome
    • A. Rich, E.F. Eikenberry, and L.I. Malkin Experiments on hemoglobin polypeptide chain initiation and on the shielding actionof the ribosome Cold Spring Harbor Symp. Quant. Biol. 31 1966 303 310
    • (1966) Cold Spring Harbor Symp. Quant. Biol. , vol.31 , pp. 303-310
    • Rich, A.1    Eikenberry, E.F.2    Malkin, L.I.3
  • 159
    • 0015505522 scopus 로고
    • Removal of formyl-methionine residue from nascent bacteriophage f2 protein
    • D. Housman, D. Gillespie, and H.F. Lodish Removal of formyl-methionine residue from nascent bacteriophage f2 protein J. Mol. Biol. 65 1972 163 166
    • (1972) J. Mol. Biol. , vol.65 , pp. 163-166
    • Housman, D.1    Gillespie, D.2    Lodish, H.F.3
  • 160
    • 0033528708 scopus 로고    scopus 로고
    • Design and synthesis of substrate analogue inhibitors of peptide deformylase
    • T. Meinnel, L. Patiny, S. Ragusa, and S. Blanquet Design and synthesis of substrate analogue inhibitors of peptide deformylase Biochemistry 38 1999 4287 4295
    • (1999) Biochemistry , vol.38 , pp. 4287-4295
    • Meinnel, T.1    Patiny, L.2    Ragusa, S.3    Blanquet, S.4
  • 161
    • 0033603628 scopus 로고    scopus 로고
    • Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin
    • S. Ragusa, P. Mouchet, C. Lazennec, V. Dive, and T. Meinnel Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin J. Mol. Biol. 289 1999 1445 1457
    • (1999) J. Mol. Biol. , vol.289 , pp. 1445-1457
    • Ragusa, S.1    Mouchet, P.2    Lazennec, C.3    Dive, V.4    Meinnel, T.5
  • 163
    • 4944246094 scopus 로고    scopus 로고
    • Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
    • L. Ferbitz, T. Maier, H. Patzelt, B. Bukau, E. Deuerling, and N. Ban Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins Nature 431 2004 590 596
    • (2004) Nature , vol.431 , pp. 590-596
    • Ferbitz, L.1    Maier, T.2    Patzelt, H.3    Bukau, B.4    Deuerling, E.5    Ban, N.6
  • 166
    • 0030004178 scopus 로고    scopus 로고
    • The C-terminal domain of peptide deformylase is disordered and dispensable for activity
    • T. Meinnel, C. Lazennec, F. Dardel, J.M. Schmitter, and S. Blanquet The C-terminal domain of peptide deformylase is disordered and dispensable for activity FEBS Lett. 385 1996 91 95
    • (1996) FEBS Lett. , vol.385 , pp. 91-95
    • Meinnel, T.1    Lazennec, C.2    Dardel, F.3    Schmitter, J.M.4    Blanquet, S.5
  • 167
    • 84902846778 scopus 로고    scopus 로고
    • Interplay between trigger factor and other protein biogenesis factors on the ribosome
    • T. Bornemann, W. Holtkamp, and W. Wintermeyer Interplay between trigger factor and other protein biogenesis factors on the ribosome Nat. Commun. 5 2014 4180
    • (2014) Nat. Commun. , vol.5 , pp. 4180
    • Bornemann, T.1    Holtkamp, W.2    Wintermeyer, W.3
  • 168
    • 0014323081 scopus 로고
    • Protein chain initiation and deformylation in B. subtilis homogenates
    • M. Takeda, and R.E. Webster Protein chain initiation and deformylation in B. subtilis homogenates Proc. Natl. Acad. Sci. U. S. A. 60 1968 1487 1494
    • (1968) Proc. Natl. Acad. Sci. U. S. A. , vol.60 , pp. 1487-1494
    • Takeda, M.1    Webster, R.E.2
  • 173
    • 23044479363 scopus 로고    scopus 로고
    • Processed N-termini of mature proteins in higher eukaryotes and their major contribution to dynamic proteomics
    • T. Meinnel, P. Peynot, and C. Giglione Processed N-termini of mature proteins in higher eukaryotes and their major contribution to dynamic proteomics Biochimie 87 2005 701 712
    • (2005) Biochimie , vol.87 , pp. 701-712
    • Meinnel, T.1    Peynot, P.2    Giglione, C.3
  • 174
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • X. Robert, and P. Gouet Deciphering key features in protein structures with the new ENDscript server Nucleic Acids Res. 42 2014 W320 W324
    • (2014) Nucleic Acids Res. , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2
  • 175
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures
    • M. Landau, I. Mayrose, Y. Rosenberg, F. Glaser, E. Martz, T. Pupko, and N. Ben-Tal ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures Nucleic Acids Res. 33 2005 W299 W302
    • (2005) Nucleic Acids Res. , vol.33 , pp. W299-W302
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5    Pupko, T.6    Ben-Tal, N.7
  • 176
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • H. Ashkenazy, E. Erez, E. Martz, T. Pupko, and N. Ben-Tal ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids Nucleic Acids Res. 38 2010 W529 W533
    • (2010) Nucleic Acids Res. , vol.38 , pp. W529-W533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5


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