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Volumn 96, Issue 4, 2009, Pages 183-188

N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition

Author keywords

BirA; Domains; Holocarboxylase synthetase; p67; Propionyl CoA carboxylase

Indexed keywords

ARGININE; BIOTIN; CARBOXYLASE; HISTONE; HOLOCARBOXYLASE SYNTHETASE; PROPIONYL COENZYME A CARBOXYLASE; PROTEIN P67; SERINE; UNCLASSIFIED DRUG;

EID: 61849137804     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2008.12.006     Document Type: Article
Times cited : (27)

References (43)
  • 1
    • 34247131876 scopus 로고    scopus 로고
    • Biotin
    • Bowman B.A., and Russell R.M. (Eds), International Life Sciences Institute, Washington, DC
    • Camporeale G., and Zempleni J. Biotin. In: Bowman B.A., and Russell R.M. (Eds). Present Knowledge in Nutrition. ninth ed. (2006), International Life Sciences Institute, Washington, DC 314-326
    • (2006) Present Knowledge in Nutrition. ninth ed. , pp. 314-326
    • Camporeale, G.1    Zempleni, J.2
  • 4
    • 43249096338 scopus 로고    scopus 로고
    • Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3
    • Kobza K., Sarath G., and Zempleni J. Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3. BMB Reports 41 (2008) 310-315
    • (2008) BMB Reports , vol.41 , pp. 310-315
    • Kobza, K.1    Sarath, G.2    Zempleni, J.3
  • 5
    • 33645053801 scopus 로고    scopus 로고
    • Lysine residues in N- and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase
    • Chew Y.C., Camporeale G., Kothapalli N., Sarath G., and Zempleni J. Lysine residues in N- and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase. J. Nutr. Biochem. 17 (2006) 225-233
    • (2006) J. Nutr. Biochem. , vol.17 , pp. 225-233
    • Chew, Y.C.1    Camporeale, G.2    Kothapalli, N.3    Sarath, G.4    Zempleni, J.5
  • 6
    • 33745660651 scopus 로고    scopus 로고
    • Biotinylation of K8 and K12 co-occurs with acetylation and mono-methylation in human histone H4
    • (abstract)
    • Chew Y.C., Raza A.S., Sarath G., and Zempleni J. Biotinylation of K8 and K12 co-occurs with acetylation and mono-methylation in human histone H4. FASEB J. 20 (2006) A610 (abstract)
    • (2006) FASEB J. , vol.20
    • Chew, Y.C.1    Raza, A.S.2    Sarath, G.3    Zempleni, J.4
  • 7
    • 33751079894 scopus 로고    scopus 로고
    • Drosophila holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan and heat tolerance
    • Camporeale G., Giordano E., Rendina R., Zempleni J., and Eissenberg J.C. Drosophila holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan and heat tolerance. J. Nutr. 136 (2006) 2735-2742
    • (2006) J. Nutr. , vol.136 , pp. 2735-2742
    • Camporeale, G.1    Giordano, E.2    Rendina, R.3    Zempleni, J.4    Eissenberg, J.C.5
  • 8
    • 34247168395 scopus 로고    scopus 로고
    • Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogasteru are caused by decreased biotinylation of histones, not of carboxylases
    • Camporeale G., Zempleni J., and Eissenberg J.C. Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogasteru are caused by decreased biotinylation of histones, not of carboxylases. J. Nutr. 137 (2007) 885-889
    • (2007) J. Nutr. , vol.137 , pp. 885-889
    • Camporeale, G.1    Zempleni, J.2    Eissenberg, J.C.3
  • 9
    • 43249125904 scopus 로고    scopus 로고
    • Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locus
    • Gralla M., Camporeale G., and Zempleni J. Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locus. J. Nutr. Biochem. 19 (2008) 400-408
    • (2008) J. Nutr. Biochem. , vol.19 , pp. 400-408
    • Gralla, M.1    Camporeale, G.2    Zempleni, J.3
  • 10
  • 11
    • 26444459387 scopus 로고    scopus 로고
    • Biotinylation of K12 in histone H4 decreases in response to DNA double strand breaks in human JAr choriocarcinoma cells
    • Kothapalli N., Sarath G., and Zempleni J. Biotinylation of K12 in histone H4 decreases in response to DNA double strand breaks in human JAr choriocarcinoma cells. J. Nutr. 135 (2005) 2337-2342
    • (2005) J. Nutr. , vol.135 , pp. 2337-2342
    • Kothapalli, N.1    Sarath, G.2    Zempleni, J.3
  • 15
    • 0347917296 scopus 로고    scopus 로고
    • Reduced histone biotinylation in multiple carboxylase deficiency patients: a nuclear role for holocarboxylase synthetase
    • Narang M.A., Dumas R., Ayer L.M., and Gravel R.A. Reduced histone biotinylation in multiple carboxylase deficiency patients: a nuclear role for holocarboxylase synthetase. Hum. Mol. Genet. 13 (2004) 15-23
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 15-23
    • Narang, M.A.1    Dumas, R.2    Ayer, L.M.3    Gravel, R.A.4
  • 16
    • 0026666377 scopus 로고
    • Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains
    • Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., and Matthews B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc Natl Acad Sci USA 89 (1992) 9257-9261
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9257-9261
    • Wilson, K.P.1    Shewchuk, L.M.2    Brennan, R.G.3    Otsuka, A.J.4    Matthews, B.W.5
  • 17
    • 0035188539 scopus 로고    scopus 로고
    • The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity
    • Chapman-Smith A., Mulhern T.D., Whelan F., Cronan Jr. J.E., and Wallace J.C. The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity. Protein Sci 10 (2001) 2608-2617
    • (2001) Protein Sci , vol.10 , pp. 2608-2617
    • Chapman-Smith, A.1    Mulhern, T.D.2    Whelan, F.3    Cronan Jr., J.E.4    Wallace, J.C.5
  • 18
    • 0028093290 scopus 로고
    • Sequence requirements for the biotinylation of carboxyl-terminal fragments of human propionyl-CoA carboxylase alpha subunit expressed in Escherichia coli
    • Leon-Del-Rio A., and Gravel R.A. Sequence requirements for the biotinylation of carboxyl-terminal fragments of human propionyl-CoA carboxylase alpha subunit expressed in Escherichia coli. J. Biol. Chem. 269 (1994) 22964-22968
    • (1994) J. Biol. Chem. , vol.269 , pp. 22964-22968
    • Leon-Del-Rio, A.1    Gravel, R.A.2
  • 19
    • 0032930647 scopus 로고    scopus 로고
    • Molecular biology of biotin attachment to proteins
    • Chapman-Smith A., and Cronan J.E.J. Molecular biology of biotin attachment to proteins. J. Nutr. 129 (1999) 477S-484S
    • (1999) J. Nutr. , vol.129
    • Chapman-Smith, A.1    Cronan, J.E.J.2
  • 20
    • 0035853728 scopus 로고    scopus 로고
    • Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase. Influence of the N-terminus on biotinylation and identification of a minimum functional protein
    • Campeau E., and Gravel R.A. Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase. Influence of the N-terminus on biotinylation and identification of a minimum functional protein. J. Biol. Chem. 276 (2001) 12310-12316
    • (2001) J. Biol. Chem. , vol.276 , pp. 12310-12316
    • Campeau, E.1    Gravel, R.A.2
  • 22
    • 38549141229 scopus 로고    scopus 로고
    • Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre
    • Bennett-Lovsey R.M., Herbert A.D., Sternberg M.J., and Kelley L.A. Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. Proteins 70 (2008) 611-625
    • (2008) Proteins , vol.70 , pp. 611-625
    • Bennett-Lovsey, R.M.1    Herbert, A.D.2    Sternberg, M.J.3    Kelley, L.A.4
  • 23
    • 0035190710 scopus 로고    scopus 로고
    • Competing protein-protein interactions are proposed to control the biological switch of the E. coli biotin repressor
    • Weaver L.H., Kwon K., Beckett D., and Matthews B.W. Competing protein-protein interactions are proposed to control the biological switch of the E. coli biotin repressor. Protein Sci. 10 (2001) 2618-2622
    • (2001) Protein Sci. , vol.10 , pp. 2618-2622
    • Weaver, L.H.1    Kwon, K.2    Beckett, D.3    Matthews, B.W.4
  • 24
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W.R., and Lipman D.J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85 (1988) 2444-2448
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 25
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • (Suppl.)
    • Bates P.A., Kelley L.A., MacCallum R.M., and Sternberg M.J. Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins 5 (2001) 39-46 (Suppl.)
    • (2001) Proteins , vol.5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.4
  • 26
    • 47249091778 scopus 로고    scopus 로고
    • Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate
    • Bagautdinov B., Matsuura Y., Bagautdinova S., and Kunishima N. Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate. J. Biol. Chem. 283 (2008) 14739-14750
    • (2008) J. Biol. Chem. , vol.283 , pp. 14739-14750
    • Bagautdinov, B.1    Matsuura, Y.2    Bagautdinova, S.3    Kunishima, N.4
  • 29
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 30
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S., and Song O. A novel genetic system to detect protein-protein interactions. Nature 340 (1989) 245-246
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 31
    • 0029092610 scopus 로고
    • Correlation of two-hybrid affinity data with in vitro measurements
    • Estojak J., Brent R., and Golemis E.A. Correlation of two-hybrid affinity data with in vitro measurements. Mol. Cell Biol. 15 (1995) 5820-5829
    • (1995) Mol. Cell Biol. , vol.15 , pp. 5820-5829
    • Estojak, J.1    Brent, R.2    Golemis, E.A.3
  • 32
    • 0035932977 scopus 로고    scopus 로고
    • Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator
    • Weaver L.H., Kwon K., Beckett D., and Matthews B.W. Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator. Proc. Natl. Acad. Sci. USA 98 (2001) 6045-6050
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6045-6050
    • Weaver, L.H.1    Kwon, K.2    Beckett, D.3    Matthews, B.W.4
  • 33
    • 0028796669 scopus 로고
    • Biotinylation of biotinidase following incubation with biocytin
    • Hymes J., Fleischhauer K., and Wolf B. Biotinylation of biotinidase following incubation with biocytin. Clin. Chim. Acta 233 (1995) 39-45
    • (1995) Clin. Chim. Acta , vol.233 , pp. 39-45
    • Hymes, J.1    Fleischhauer, K.2    Wolf, B.3
  • 34
    • 0028858269 scopus 로고
    • Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency
    • Hymes J., Fleischhauer K., and Wolf B. Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency. Biochem. Mol. Med. 56 (1995) 76-83
    • (1995) Biochem. Mol. Med. , vol.56 , pp. 76-83
    • Hymes, J.1    Fleischhauer, K.2    Wolf, B.3
  • 35
    • 0032906144 scopus 로고    scopus 로고
    • Human biotinidase isn't just for recycling biotin
    • Hymes J., and Wolf B. Human biotinidase isn't just for recycling biotin. J. Nutr. 129 (1999) 485S-489S
    • (1999) J. Nutr. , vol.129
    • Hymes, J.1    Wolf, B.2
  • 36
    • 34548460599 scopus 로고    scopus 로고
    • Three dimensional structure of human biotinidase: computer modeling and functional correlations
    • Pindolia K., Jensen K., and Wolf B. Three dimensional structure of human biotinidase: computer modeling and functional correlations. Mol. Genet. Metab. 92 (2007) 13-22
    • (2007) Mol. Genet. Metab. , vol.92 , pp. 13-22
    • Pindolia, K.1    Jensen, K.2    Wolf, B.3
  • 37
    • 33745642479 scopus 로고    scopus 로고
    • Epigenetic regulation of chromatin structure and gene function by biotin
    • Hassan Y.I., and Zempleni J. Epigenetic regulation of chromatin structure and gene function by biotin. J. Nutr. 136 (2006) 1763-1765
    • (2006) J. Nutr. , vol.136 , pp. 1763-1765
    • Hassan, Y.I.1    Zempleni, J.2
  • 38
    • 61849124381 scopus 로고    scopus 로고
    • A tyrosine kinase is involved in the nuclear translocation of human holocarboxylase synthetase
    • San Diego, CA, Abstract C119
    • Y.I. Hassan, J. Zempleni, A tyrosine kinase is involved in the nuclear translocation of human holocarboxylase synthetase, Experimental Biology Meeting, San Diego, CA, Abstract C119, number 691.14 (2008).
    • (2008) Experimental Biology Meeting , vol.691 , Issue.14
    • Hassan, Y.I.1    Zempleni, J.2
  • 39
    • 48349106280 scopus 로고    scopus 로고
    • Epigenetic regulation of chromatin structure and gene function by biot: are biotin requirements being met?
    • Zempleni J., Chew Y.C., Hassan Y.I., and Wijeratne S.S.K. Epigenetic regulation of chromatin structure and gene function by biot: are biotin requirements being met?. Nutr. Rev. 66 (2008) S46-S48
    • (2008) Nutr. Rev. , vol.66
    • Zempleni, J.1    Chew, Y.C.2    Hassan, Y.I.3    Wijeratne, S.S.K.4
  • 40
    • 25444442591 scopus 로고    scopus 로고
    • Mutations in the holocarboxylase synthetase gene HLCS
    • Suzuki Y., Yang X., Aoki Y., Kure S., and Matsubara Y. Mutations in the holocarboxylase synthetase gene HLCS. Hum. Mutat. 26 (2005) 285-290
    • (2005) Hum. Mutat. , vol.26 , pp. 285-290
    • Suzuki, Y.1    Yang, X.2    Aoki, Y.3    Kure, S.4    Matsubara, Y.5
  • 41
    • 0032809640 scopus 로고    scopus 로고
    • Mechanism of biotin responsiveness in biotin-responsive multiple carboxylase deficiency
    • Dupuis L., Campeau E., Leclerc D., and Gravel R.A. Mechanism of biotin responsiveness in biotin-responsive multiple carboxylase deficiency. Molec. Genet. Metabol. 66 (1999) 80-90
    • (1999) Molec. Genet. Metabol. , vol.66 , pp. 80-90
    • Dupuis, L.1    Campeau, E.2    Leclerc, D.3    Gravel, R.A.4
  • 42
    • 0033769643 scopus 로고    scopus 로고
    • Lipoylating and biotinylating enzymes contain a homologous catalytic module
    • Reche P.A. Lipoylating and biotinylating enzymes contain a homologous catalytic module. Protein Sci. 9 (2000) 1922-1929
    • (2000) Protein Sci. , vol.9 , pp. 1922-1929
    • Reche, P.A.1
  • 43
    • 0034683161 scopus 로고    scopus 로고
    • Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase
    • Reche P.A., Howard M.J., Broadhurst R.W., and Perham R.N. Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase. FEBS Lett. 479 (2000) 93-98
    • (2000) FEBS Lett. , vol.479 , pp. 93-98
    • Reche, P.A.1    Howard, M.J.2    Broadhurst, R.W.3    Perham, R.N.4


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