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Volumn 38, Issue 3, 2011, Pages 197-203

Protein post-translational modification in prokaryotes

Author keywords

Acetylation; Glycosylation; Lipid modification; Methylation; Phosphorylation; Post translational modification; Prokaryote; Ubiquitin like modification

Indexed keywords

MYCOBACTERIUM TUBERCULOSIS; PROKARYOTA; SALMONELLA ENTERICA;

EID: 79955831164     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: 10.3724/SP.J.1206.2010.00138     Document Type: Article
Times cited : (1)

References (36)
  • 1
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in Archaea
    • DOI 10.1128/MMBR.69.3.393-425.2005
    • Eichler J, Adams M W. Posttranslational protein modification in Archaea. Microbiol Mol Biol Rev, 2005, 69(3):393-425 (Pubitemid 41306744)
    • (2005) Microbiology and Molecular Biology Reviews , vol.69 , Issue.3 , pp. 393-425
    • Eichler, J.1    Adams, M.W.W.2
  • 2
    • 35348970382 scopus 로고    scopus 로고
    • Celebrating the golden anniversary of the discovery of bacillosamine, the diamino sugar of a Bacillus
    • DOI 10.1093/glycob/cwm089
    • Sharon N. Celebrating the golden anniversary of the discovery of bacillosamine, the diamino sugar of a Bacillus. Glycobiology, 2007, 17(11):1150-1155 (Pubitemid 47604722)
    • (2007) Glycobiology , vol.17 , Issue.11 , pp. 1150-1155
    • Sharon, N.1
  • 3
    • 33646564396 scopus 로고    scopus 로고
    • Definition of the bacterial N-glycosylation site consensus sequence
    • Kowarik M, Young N M, Numao S, et al. Definition of the bacterial N-glycosylation site consensus sequence. EMBO J, 2006, 25(9):1957-1966
    • (2006) EMBO J. , vol.25 , Issue.9 , pp. 1957-1966
    • Kowarik, M.1    Young, N.M.2    Numao, S.3
  • 4
    • 0024346543 scopus 로고
    • Structure and biosynthesis of prokaryotic glycoproteins
    • Lechner J, Wieland F. Structure and biosynthesis of prokaryotic glycoproteins. Annu Rev Biochem, 1989, 58:173-194 (Pubitemid 19172968)
    • (1989) Annual Review of Biochemistry , vol.58 , pp. 173-194
    • Lechner, J.1    Wieland, F.2
  • 7
    • 0028987131 scopus 로고
    • Lipoproteins of gram-positive bacteria
    • Sutcliffe I C, Russell R R. Lipoproteins of gram-positive bacteria. J Bacteriol, 1995, 177(5):1123-1128
    • (1995) J. Bacteriol. , vol.177 , Issue.5 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.2
  • 8
    • 0034832009 scopus 로고    scopus 로고
    • Post-translational modification of the S-layer glycoprotein occurs following translocation across the plasma membrane of the haloarchaeon Haloferax volcanii
    • DOI 10.1046/j.1432-1327.2001.02361.x
    • Eichler J. Post-translational modification of the S-layer glycoprotein occurs following translocation across the plasma membrane of the haloarchaeon Haloferax volcanii. Eur J Biochem, 2001, 268(15):4366-4373 (Pubitemid 32862899)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.15 , pp. 4366-4373
    • Eichler, J.1
  • 9
    • 4344618574 scopus 로고    scopus 로고
    • Ancestral lipid biosynthesis and early membrane evolution
    • DOI 10.1016/j.tibs.2004.07.002, PII S0968000404001574
    • Pereto J, Lopez-Garcia P, Moreira D. Ancestral lipid biosynthesis and early membrane evolution. Trends Biochem Sci, 2004, 29(9):469-477 (Pubitemid 39158870)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.9 , pp. 469-477
    • Pereto, J.1    Lopez-Garcia, P.2    Moreira, D.3
  • 10
    • 0035049164 scopus 로고    scopus 로고
    • Post-translational GPI lipid anchor modification of proteins in kingdoms of life: Analysis of protein sequence data from complete genomes
    • Eisenhaber B, Bork P, Eisenhaber F. Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes. Protein Eng, 2001, 14(1):17-25 (Pubitemid 32318934)
    • (2001) Protein Engineering , vol.14 , Issue.1 , pp. 17-25
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 11
    • 34447272508 scopus 로고    scopus 로고
    • PelC is a Pseudomonas aeruginosa outer membrane lipoprotein of the OMA family of proteins involved in exopolysaccharide transport
    • DOI 10.1016/j.biochi.2007.04.002, PII S0300908407000971
    • Vasseur P, Soscia C, Voulhoux R, et al. PelC is a Pseudomonas aeruginosa outer membrane lipoprotein of the OMA family of proteins involved in exopolysaccharide transport. Biochimie, 2007, 89(8):903-915 (Pubitemid 47039273)
    • (2007) Biochimie , vol.89 , Issue.8 , pp. 903-915
    • Vasseur, P.1    Soscia, C.2    Voulhoux, R.3    Filloux, A.4
  • 12
    • 0034692923 scopus 로고    scopus 로고
    • Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: Unusual amino acid modification, conservation and adaptation
    • Grabarse W, Mahlert F, Shima S, et al. Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation. J Mol Biol, 2000, 303(2):329-344
    • (2000) J. Mol. Biol. , vol.303 , Issue.2 , pp. 329-344
    • Grabarse, W.1    Mahlert, F.2    Shima, S.3
  • 13
    • 0028533719 scopus 로고
    • Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus
    • Baumann H, Knapp S, Lundback T, et al. Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Nat Struct Biol, 1994, 1(11):808-819
    • (1994) Nat. Struct Biol. , vol.1 , Issue.11 , pp. 808-819
    • Baumann, H.1    Knapp, S.2    Lundback, T.3
  • 14
    • 76449114765 scopus 로고    scopus 로고
    • High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans
    • Cao X J, Dai J, Xu H, et al. High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans. Cell Res, 2010, 20(2):197-210
    • (2010) Cell. Res. , vol.20 , Issue.2 , pp. 197-210
    • Cao, X.J.1    Dai, J.2    Xu, H.3
  • 15
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation: An emerging regulator of protein function
    • DOI 10.1016/j.molcel.2005.04.003, PII S1097276505012475
    • Bedford M T, Richard S. Arginine methylation an emerging regulator of protein function. Mol Cell, 2005, 18(3):263-272 (Pubitemid 41350532)
    • (2005) Molecular Cell , vol.18 , Issue.3 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 16
    • 33846978445 scopus 로고    scopus 로고
    • Enzymatic methylation of the Mycobacterium tuberculosis heparin-binding haemagglutinin
    • Host H, Drobecq H, Locht C, et al. Enzymatic methylation of the Mycobacterium tuberculosis heparin-binding haemagglutinin. FEMS Microbiol Lett, 2007, 268(2):144-150
    • (2007) FEMS Microbiol. Lett. , vol.268 , Issue.2 , pp. 144-150
    • Host, H.1    Drobecq, H.2    Locht, C.3
  • 17
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson J S, Kofoid E C. Communication modules in bacterial signaling proteins. Annu Rev Genet, 1992, 26:71-112 (Pubitemid 23022604)
    • (1992) Annual Review of Genetics , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 18
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma P W, Lengeler J W, Jacobson G R. Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol Rev, 1993, 57(3):543-594 (Pubitemid 23262509)
    • (1993) Microbiological Reviews , vol.57 , Issue.3 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 19
    • 0015517248 scopus 로고
    • Phosphorylation of ribosomal proteins of Escherichia coli by protein kinase from rabbit skeletal muscle
    • Traugh J A, Traut R R. Phosphorylation of ribosomal proteins of Escherichia coli by protein kinase from rabbit skeletal muscle. Biochemistry, 1972, 11(13):2503-2509
    • (1972) Biochemistry , vol.11 , Issue.13 , pp. 2503-2509
    • Traugh, J.A.1    Traut, R.R.2
  • 20
    • 38949118022 scopus 로고    scopus 로고
    • PhoP-PhoP interaction at adjacent PhoP binding sites is influenced by protein phosphorylation
    • DOI 10.1128/JB.01074-07
    • Sinha A, Gupta S, Bhutani S, et al. PhoP-PhoP interaction at adjacent PhoP binding sites is influenced by protein phosphorylation. J Bacteriol, 2008, 190(4):1317-1328 (Pubitemid 351215013)
    • (2008) Journal of Bacteriology , vol.190 , Issue.4 , pp. 1317-1328
    • Sinha, A.1    Gupta, S.2    Bhutani, S.3    Pathak, A.4    Sarkar, D.5
  • 21
    • 33645307109 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis
    • Walters S B, Dubnau E, Kolesnikova I, et al. The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosynthesis. Mol Microbiol, 2006, 60(2):312-330
    • (2006) Mol. Microbiol. , vol.60 , Issue.2 , pp. 312-330
    • Walters, S.B.1    Dubnau, E.2    Kolesnikova, I.3
  • 22
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of Rna synthesis
    • Allfrey VG, Faulkner R, Mirsky AE. Acetylation and methylation of histones and their possible role in the regulation of Rna synthesis. Proc Natl Acad Sci USA, 1964, 51(5):786-794
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , Issue.5 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 23
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • DOI 10.1126/science.1077650
    • Starai V J, Celic I, Cole R N, et al. Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science, 2002, 298(5602):2390-2392 (Pubitemid 36014212)
    • (2002) Science , vol.298 , Issue.5602 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 24
    • 0037023326 scopus 로고    scopus 로고
    • The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation
    • DOI 10.1126/science.1070506
    • Bell S D, Botting C H, Wardleworth B N, et al. The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation. Science, 2002, 296(5565):148-151 (Pubitemid 34280075)
    • (2002) Science , vol.296 , Issue.5565 , pp. 148-151
    • Bell, S.D.1    Botting, C.H.2    Wardleworth, B.N.3    Jackson, S.P.4    White, M.F.5
  • 25
    • 20444427964 scopus 로고    scopus 로고
    • Sir2 and the acetyltransferase, Pat, regulate the archaeal chromatin protein, Alba
    • DOI 10.1074/jbc.M501280200
    • Marsh V L, Peak-Chew S Y, Bell S D. Sir2 and the acetyltransferase, Pat, regulate the archaeal chromatin protein, Alba. J Biol Chem, 2005, 280(22):21122-21128 (Pubitemid 40805672)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 21122-21128
    • Marsh, V.L.1    Peak-Chew, S.Y.2    Bell, S.D.3
  • 26
    • 0024381096 scopus 로고
    • Cloning and molecular characterization of the gene rimL which encodes an enzyme acetylating ribosomal protein L12 of Escherichia coli K12
    • Tanaka S, Matsushita Y, Yoshikawa A, et al. Cloning and molecular characterization of the gene rimL which encodes an enzyme acetylating ribosomal protein L12 of Escherichia coli K12. Mol Gen Genet, 1989, 217 (2-3): 289-293 (Pubitemid 19165009)
    • (1989) Molecular and General Genetics , vol.217 , Issue.2-3 , pp. 289-293
    • Tanaka, S.1    Matsushita, Y.2    Yoshikawa, A.3    Isono, K.4
  • 27
    • 0037108102 scopus 로고    scopus 로고
    • GTPase activation of elongation factors Tu and G on the ribosome
    • Mohr D, Wintermeyer W, Rodnina M V. GTPase activation of elongation factors Tu and G on the ribosome. Biochemistry, 2002, 41(41):12520-12528
    • (2002) Biochemistry , vol.41 , Issue.41 , pp. 12520-12528
    • Mohr, D.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 28
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang Q, Zhang Y, Yang C, et al. Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science, 2010, 327(5968):1004-1007
    • (2010) Science , vol.327 , Issue.5968 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3
  • 30
    • 67649391054 scopus 로고    scopus 로고
    • Prokaryotic ubiquitin-like protein (Pup), proteasomes and pathogenesis
    • Darwin K H. Prokaryotic ubiquitin-like protein (Pup), proteasomes and pathogenesis. Nat Rev Microbiol, 2009, 7(7):485-491
    • (2009) Nat. Rev. Microbiol. , vol.7 , Issue.7 , pp. 485-491
    • Darwin, K.H.1
  • 31
    • 56449118262 scopus 로고    scopus 로고
    • Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis
    • Pearce M J, Mintseris J, Ferreyra J, et al. Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science, 2008, 322(5904):1104-1107
    • (2008) Science , vol.322 , Issue.5904 , pp. 1104-1107
    • Pearce, M.J.1    Mintseris, J.2    Ferreyra, J.3
  • 32
    • 67349193285 scopus 로고    scopus 로고
    • Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
    • Striebel F, Imkamp F, Sutter M, et al. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat Struct Mol Biol, 2009, 16(6):647-651
    • (2009) Nat. Struct Mol. Biol. , vol.16 , Issue.6 , pp. 647-651
    • Striebel, F.1    Imkamp, F.2    Sutter, M.3
  • 33
    • 75149113560 scopus 로고    scopus 로고
    • Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo
    • Imkamp F, Rosenberger T, Striebel F, et al. Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo. Mol Microbiol, 2010, 75(3):744-754
    • (2010) Mol. Microbiol. , vol.75 , Issue.3 , pp. 744-754
    • Imkamp, F.1    Rosenberger, T.2    Striebel, F.3
  • 34
    • 66249133911 scopus 로고    scopus 로고
    • Solution structure of SUMO from Trypanosoma brucei and its interaction with Ubc9
    • Shang Q, Xu C, Zhang J, et al. Solution structure of SUMO from Trypanosoma brucei and its interaction with Ubc9. Proteins, 2009, 76(1):266-269
    • (2009) Proteins , vol.76 , Issue.1 , pp. 266-269
    • Shang, Q.1    Xu, C.2    Zhang, J.3
  • 35
    • 70149094758 scopus 로고    scopus 로고
    • Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein
    • Liao S, Shang Q, Zhang X, et al. Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein. Biochem J, 2009, 422(2):207-215
    • (2009) Biochem. J. , vol.422 , Issue.2 , pp. 207-215
    • Liao, S.1    Shang, Q.2    Zhang, X.3
  • 36
    • 77649151706 scopus 로고    scopus 로고
    • Prokaryotic ubiquitinlike protein (Pup) proteome of Mycobacterium tuberculosis
    • Festa R A, McAllister F, Pearce M J, et al. Prokaryotic ubiquitinlike protein (Pup) proteome of Mycobacterium tuberculosis. PLoS One, 2009, 5(1): e8589
    • (2009) PLoS One , vol.5 , Issue.1
    • Festa, R.A.1    McAllister, F.2    Pearce, M.J.3


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