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Volumn 419, Issue 3-4, 2012, Pages 223-233

Functional versatility of a single protein surface in two protein:Protein interactions

Author keywords

bispecificity; evolution; protein:protein interactions; surface loops

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; BACTERIAL PROTEIN; BIOTIN; PROTEIN BIRA; UNCLASSIFIED DRUG;

EID: 84860721058     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.03.010     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 77953108542 scopus 로고    scopus 로고
    • The diversity of ubiquitin recognition: Hot spots and varied specificity
    • Winget J.M., and Mayor T. The diversity of ubiquitin recognition: hot spots and varied specificity Mol. Cell 38 2010 627 635
    • (2010) Mol. Cell , vol.38 , pp. 627-635
    • Winget, J.M.1    Mayor, T.2
  • 2
    • 79952093554 scopus 로고    scopus 로고
    • Multispecific recognition: Mechanism, evolution, and design
    • Erijman A., Aizner Y., and Shifman J.M. Multispecific recognition: mechanism, evolution, and design Biochemistry 50 2011 602 611
    • (2011) Biochemistry , vol.50 , pp. 602-611
    • Erijman, A.1    Aizner, Y.2    Shifman, J.M.3
  • 3
    • 0019473758 scopus 로고
    • Genetic and biochemical characterization of the birA gene and its product: Evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli
    • DOI 10.1016/0022-2836(81)90043-7
    • Barker D.F., and Campbell A.M. Genetic and biochemical characterization of the birA gene and its product: evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli J. Mol. Biol. 146 1981 469 492 (Pubitemid 11100438)
    • (1981) Journal of Molecular Biology , vol.146 , Issue.4 , pp. 469-492
    • Barker, D.F.1    Campbell, A.M.2
  • 4
    • 0019482402 scopus 로고
    • The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase
    • DOI 10.1016/0022-2836(81)90042-5
    • Barker D.F., and Campbell A.M. The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase J. Mol. Biol. 146 1981 451 467 (Pubitemid 11100437)
    • (1981) Journal of Molecular Biology , vol.146 , Issue.4 , pp. 451-467
    • Barker, D.F.1    Campbell, A.M.2
  • 5
    • 0023679220 scopus 로고
    • Expression of the biotin biosynthetic operon of Escherichia coli is regulated by the rate of protein biotination
    • Cronan J.E. Expression of the biotin biosynthetic operon of Escherichia coli is regulated by the rate of protein biotination J. Biol. Chem. 263 1988 10332 10336
    • (1988) J. Biol. Chem. , vol.263 , pp. 10332-10336
    • Cronan, J.E.1
  • 6
    • 0027389215 scopus 로고
    • Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis
    • Li S.J., and Cronan J.E. Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis J. Bacteriol. 175 1993 332 340
    • (1993) J. Bacteriol. , vol.175 , pp. 332-340
    • Li, S.J.1    Cronan, J.E.2
  • 7
    • 0037474538 scopus 로고    scopus 로고
    • Coupling of protein assembly and DNA binding: Biotin repressor dimerization precedes biotin operator binding
    • DOI 10.1016/S0022-2836(02)01308-6
    • Streaker E.D., and Beckett D. Coupling of protein assembly and DNA binding: biotin repressor dimerization precedes biotin operator binding J. Mol. Biol. 325 2003 937 948 (Pubitemid 36263405)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 937-948
    • Streaker, E.D.1    Beckett, D.2
  • 8
    • 0032830564 scopus 로고    scopus 로고
    • Dimerization of the Escherichia coli biotin repressor: Corepressor function in protein assembly
    • Eisenstein E., and Beckett D. Dimerization of the Escherichia coli biotin repressor: corepressor function in protein assembly Biochemistry 38 1999 13077 13084
    • (1999) Biochemistry , vol.38 , pp. 13077-13084
    • Eisenstein, E.1    Beckett, D.2
  • 9
    • 0018538322 scopus 로고
    • Biotinyl 5′-adenylate: Corepressor role in the regulation of the biotin genes of Escherichia coli K-12
    • Prakash O., and Eisenberg M.A. Biotinyl 5′-adenylate: corepressor role in the regulation of the biotin genes of Escherichia coli K-12 Proc. Natl Acad. Sci. USA 76 1979 5592 5595
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 5592-5595
    • Prakash, O.1    Eisenberg, M.A.2
  • 10
    • 0036797992 scopus 로고    scopus 로고
    • Conservation of the biotin regulon and the BirA regulatory signal in eubacteria and archaea
    • DOI 10.1101/gr.314502
    • Rodionov D.A., Mironov A.A., and Gelfand M.S. Conservation of the biotin regulon and the BirA regulatory signal in Eubacteria and Archaea Genome Res. 12 2002 1507 1516 (Pubitemid 35175088)
    • (2002) Genome Research , vol.12 , Issue.10 , pp. 1507-1516
    • Rodionov, D.A.1    Mironov, A.A.2    Gelfand, M.S.3
  • 12
    • 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
  • 13
    • 33344466006 scopus 로고    scopus 로고
    • Co-repressor induced order and biotin repressor dimerization: A case for divergent followed by convergent evolution
    • DOI 10.1016/j.jmb.2005.12.066, PII S0022283605016426
    • Wood Z.A., Weaver L.H., Brown P.H., Beckett D., and Matthews B.W. Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution J. Mol. Biol. 357 2006 509 523 (Pubitemid 43290751)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.2 , pp. 509-523
    • Wood, Z.A.1    Weaver, L.H.2    Brown, P.H.3    Beckett, D.4    Matthews, B.W.5
  • 14
    • 0029646091 scopus 로고
    • Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing
    • DOI 10.1016/S0969-2126(01)00277-5
    • Athappilly F.K., and Hendrickson W.A. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing Structure 3 1995 1407 1419 (Pubitemid 3012268)
    • (1995) Structure , vol.3 , Issue.12 , pp. 1407-1419
    • Athappilly, F.K.1    Hendrickson, W.A.2
  • 16
    • 0035190710 scopus 로고    scopus 로고
    • Competing protein:protein interactions are proposed to control the biological switch of the E. coli biotin repressor
    • DOI 10.1110/ps.ps.32701
    • 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 (Pubitemid 33091585)
    • (2001) Protein Science , vol.10 , Issue.12 , pp. 2618-2622
    • Weaver, L.H.1    Kwon, K.2    Beckett, D.3    Matthews, B.W.4
  • 17
    • 0034671258 scopus 로고    scopus 로고
    • Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor
    • DOI 10.1006/jmbi.2000.4249
    • Kwon K., Streaker E.D., Ruparelia S., and Beckett D. Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor J. Mol. Biol. 304 2000 821 833 (Pubitemid 32047085)
    • (2000) Journal of Molecular Biology , vol.304 , Issue.5 , pp. 821-833
    • Kwon, K.1    Streaker, E.D.2    Ruparelia, S.3    Beckett, D.4
  • 18
    • 0033846484 scopus 로고    scopus 로고
    • Function of a conserved sequence motif in biotin holoenzyme synthetases
    • Kwon K., and Beckett D. Function of a conserved sequence motif in biotin holoenzyme synthetases Protein Sci. 9 2000 1530 1539 (Pubitemid 30659191)
    • (2000) Protein Science , vol.9 , Issue.8 , pp. 1530-1539
    • Kwon, K.1    Beckett, D.2
  • 19
    • 65549121720 scopus 로고    scopus 로고
    • Thermodynamic and structural investigation of bispecificity in protein-protein interactions
    • Zhao H., Naganathan S., and Beckett D. Thermodynamic and structural investigation of bispecificity in protein-protein interactions J. Mol. Biol. 389 2009 336 348
    • (2009) J. Mol. Biol. , vol.389 , pp. 336-348
    • Zhao, H.1    Naganathan, S.2    Beckett, D.3
  • 20
    • 61449218735 scopus 로고    scopus 로고
    • Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity
    • Tron C.M., McNae I.W., Nutley M., Clarke D.J., Cooper A., and Walkinshaw M.D. Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity J. Mol. Biol. 387 2009 129 146
    • (2009) J. Mol. Biol. , vol.387 , pp. 129-146
    • Tron, C.M.1    McNae, I.W.2    Nutley, M.3    Clarke, D.J.4    Cooper, A.5    Walkinshaw, M.D.6
  • 21
    • 77950134712 scopus 로고    scopus 로고
    • Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration
    • Gupta V., Gupta R.K., Khare G., Salunke D.M., Surolia A., and Tyagi A.K. Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration PLoS One 5 2010 e9222
    • (2010) PLoS One , vol.5 , pp. 9222
    • Gupta, V.1    Gupta, R.K.2    Khare, G.3    Salunke, D.M.4    Surolia, A.5    Tyagi, A.K.6
  • 22
    • 0029986466 scopus 로고    scopus 로고
    • Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase
    • DOI 10.1074/jbc.271.13.7559
    • Nenortas E., and Beckett D. Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase J. Biol. Chem. 271 1996 7559 7567 (Pubitemid 26107032)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.13 , pp. 7559-7567
    • Nenortas, E.1    Beckett, D.2
  • 23
    • 0028307533 scopus 로고
    • Kinetics of biotinyl-5'-adenylate synthesis catalyzed by the Escherichia coli repressor of biotin biosynthesis and the stability of the enzyme- product complex
    • DOI 10.1021/bi00189a041
    • Xu Y., and Beckett D. Kinetics of biotinyl-5′-adenylate synthesis catalyzed by the Escherichia coli repressor of biotin biosynthesis and the stability of the enzyme-product complex Biochemistry 33 1994 7354 7360 (Pubitemid 24208775)
    • (1994) Biochemistry , vol.33 , Issue.23 , pp. 7354-7360
    • Xu, Y.1    Beckett, D.2
  • 24
    • 79953898209 scopus 로고    scopus 로고
    • Biotinylation, a post-translational modification controlled by the rate of protein-protein association
    • Ingaramo M., and Beckett D. Biotinylation, a post-translational modification controlled by the rate of protein-protein association J. Biol. Chem. 286 2011 13071 13078
    • (2011) J. Biol. Chem. , vol.286 , pp. 13071-13078
    • Ingaramo, M.1    Beckett, D.2
  • 25
    • 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
  • 26
    • 80052320249 scopus 로고    scopus 로고
    • In vivo tests of thermodynamic models of transcription repressor function
    • Tungtur S., Skinner H., Zhan H., Swint-Kruse L., and Beckett D. In vivo tests of thermodynamic models of transcription repressor function Biophys. Chem. 159 2011 142 151
    • (2011) Biophys. Chem. , vol.159 , pp. 142-151
    • Tungtur, S.1    Skinner, H.2    Zhan, H.3    Swint-Kruse, L.4    Beckett, D.5
  • 27
    • 51649094321 scopus 로고    scopus 로고
    • Built-in loops allow versatility in domain-domain interactions: Lessons from self-interacting domains
    • Akiva E., Itzhaki Z., and Margalit H. Built-in loops allow versatility in domain-domain interactions: lessons from self-interacting domains Proc. Natl Acad. Sci. USA 105 2008 13292 13297
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 13292-13297
    • Akiva, E.1    Itzhaki, Z.2    Margalit, H.3
  • 30
    • 0037067765 scopus 로고    scopus 로고
    • Manipulating monomer-dimer equilibrium of bovine β-lactoglobulin by amino acid substitution
    • DOI 10.1074/jbc.M203659200
    • Sakurai K., and Goto Y. Manipulating monomer-dimer equilibrium of bovine β-lactoglobulin by amino acid substitution J. Biol. Chem. 277 2002 25735 25740 (Pubitemid 34951894)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25735-25740
    • Sakurai, K.1    Goto, Y.2
  • 31
    • 0027431496 scopus 로고
    • Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator sequence
    • Abbott J., and Beckett D. Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator sequence Biochemistry 32 1993 9649 9656 (Pubitemid 23296809)
    • (1993) Biochemistry , vol.32 , Issue.37 , pp. 9649-9656
    • Abbott, J.1    Beckett, D.2
  • 32
    • 0001453814 scopus 로고
    • The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin
    • Lane M.D., Rominger K.L., Young D.L., and Lynen F. The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin J. Biol. Chem. 239 1964 2865 2871
    • (1964) J. Biol. Chem. , vol.239 , pp. 2865-2871
    • Lane, M.D.1    Rominger, K.L.2    Young, D.L.3    Lynen, F.4
  • 33
    • 34548605606 scopus 로고    scopus 로고
    • Nucleation of an Allosteric Response via Ligand-induced Loop Folding
    • DOI 10.1016/j.jmb.2007.07.020, PII S0022283607009576
    • Naganathan S., and Beckett D. Nucleation of an allosteric response via ligand-induced loop folding J. Mol. Biol. 373 2007 96 111 (Pubitemid 47398877)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.1 , pp. 96-111
    • Naganathan, S.1    Beckett, D.2
  • 34
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 35
    • 0017107966 scopus 로고
    • Sedimentation equilibrium techniques: Multiple speed analyses and an overspeed procedure
    • Roark D.E. Sedimentation equilibrium techniques: multiple speed analyses and an overspeed procedure Biophys. Chem. 5 1976 185 196
    • (1976) Biophys. Chem. , vol.5 , pp. 185-196
    • Roark, D.E.1
  • 36
    • 0033555541 scopus 로고    scopus 로고
    • Molecular recognition in a post-translational modification of exceptional specificity
    • Chapman-Smith A., Morris T.W., Wallace J.C., and Cronan J.E. Molecular recognition in a post-translational modification of exceptional specificity J. Biol. Chem. 274 1999 1449 1457
    • (1999) J. Biol. Chem. , vol.274 , pp. 1449-1457
    • Chapman-Smith, A.1    Morris, T.W.2    Wallace, J.C.3    Cronan, J.E.4
  • 37
    • 71449118660 scopus 로고    scopus 로고
    • Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition
    • Ingaramo M., and Beckett D. Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition J. Biol. Chem. 284 2009 30862 30870
    • (2009) J. Biol. Chem. , vol.284 , pp. 30862-30870
    • Ingaramo, M.1    Beckett, D.2
  • 38
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson M.L., Correia J.J., Yphantis D.A., and Halvorson H.R. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques Biophys. J. 36 1981 575 588
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 39
    • 0029118618 scopus 로고
    • Sedimentation equilibrium as thermodynamic tool
    • Laue T.M. Sedimentation equilibrium as thermodynamic tool Methods Enzymol. 259 1995 427 452
    • (1995) Methods Enzymol. , vol.259 , pp. 427-452
    • Laue, T.M.1


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