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Volumn 35, Issue 4, 2008, Pages 711-718

Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli

Author keywords

DNA binding; Membrane binding; Multifunctional enzyme; Proline utilization; PutA; Transcriptional regulation

Indexed keywords

BACTERIAL PROTEIN; GLUTAMIC ACID; HELIX LOOP HELIX PROTEIN; MEMBRANE ENZYME; PROLINE; PROLINE DEHYDROGENASE; PROLINE UTILIZATION A PROTEIN; QUERCETIN; UNCLASSIFIED DRUG;

EID: 53849098986     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-008-0053-6     Document Type: Review
Times cited : (33)

References (31)
  • 1
    • 0021104415 scopus 로고
    • Proline dehydrogenase from Escherichia K12, properties of the membrane-associated enzyme
    • JLA Abrahamson LG Baker JT Stephenson JM Wood 1983 Proline dehydrogenase from Escherichia K12, properties of the membrane-associated enzyme Eur J Biochem 134 77 82
    • (1983) Eur J Biochem , vol.134 , pp. 77-82
    • Abrahamson, J.L.A.1    Baker, L.G.2    Stephenson, J.T.3    Wood, J.M.4
  • 2
    • 0035901522 scopus 로고    scopus 로고
    • Redox properties of the PutA protein from Escherichia coli and the influence of the flavin redox state on PutA-DNA interactions
    • DF Becker EA Thomas 2001 Redox properties of the PutA protein from Escherichia coli and the influence of the flavin redox state on PutA-DNA interactions Biochemistry 40 4714 4722
    • (2001) Biochemistry , vol.40 , pp. 4714-4722
    • Becker, D.F.1    Thomas, E.A.2
  • 3
    • 0026690379 scopus 로고
    • Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli
    • E Brown JM Wood 1992 Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli J Biol Chem 267 13086 13092
    • (1992) J Biol Chem , vol.267 , pp. 13086-13092
    • Brown, E.1    Wood, J.M.2
  • 4
    • 0027419533 scopus 로고
    • Conformational change and membrane association of the PutA protein are coincident with reduction of its FAD cofactor by proline
    • ED Brown JM Wood 1993 Conformational change and membrane association of the PutA protein are coincident with reduction of its FAD cofactor by proline J Biol Chem 268 8972 8979
    • (1993) J Biol Chem , vol.268 , pp. 8972-8979
    • Brown, E.D.1    Wood, J.M.2
  • 6
    • 0023035989 scopus 로고
    • Solubilization and functional reconstitution of the proline transport system of Escherichia coli
    • C-C Chen TH Wilson 1986 Solubilization and functional reconstitution of the proline transport system of Escherichia coli J Biol Chem 261 2599 2604
    • (1986) J Biol Chem , vol.261 , pp. 2599-2604
    • Chen, C.-C.1    Wilson, T.H.2
  • 7
    • 18244374777 scopus 로고    scopus 로고
    • Activity of Lac repressor anchored to the Escherichia coli inner membrane
    • B Görke J Reinhardt B Rak 2005 Activity of Lac repressor anchored to the Escherichia coli inner membrane Nucleic Acids Res 33 2504 2511
    • (2005) Nucleic Acids Res , vol.33 , pp. 2504-2511
    • Görke, B.1    Reinhardt, J.2    Rak, B.3
  • 8
    • 3843135240 scopus 로고    scopus 로고
    • Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzyme
    • D Gu Y Zhou V Kallhoff B Baban JJ Tanner DF Becker 2004 Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzyme J Biol Chem 279 31171 31176
    • (2004) J Biol Chem , vol.279 , pp. 31171-31176
    • Gu, D.1    Zhou, Y.2    Kallhoff, V.3    Baban, B.4    Tanner, J.J.5    Becker, D.F.6
  • 10
    • 9944225262 scopus 로고    scopus 로고
    • Molecular mechanisms for multitasking: Recent crystal structures of moonlighting proteins
    • CJ Jeffery 2004 Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins Curr Opin Struct Biol 14 663 668
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 663-668
    • Jeffery, C.J.1
  • 11
    • 21744454349 scopus 로고    scopus 로고
    • Characterization of a bifunctional PutA homologue from Bradyrhizobium japonicum and identification of an active site residue that modulates proline reduction of the flavin adenine dinucleotide cofactor
    • N Krishnan DF Becker 2005 Characterization of a bifunctional PutA homologue from Bradyrhizobium japonicum and identification of an active site residue that modulates proline reduction of the flavin adenine dinucleotide cofactor Biochemistry 44 9130 9139
    • (2005) Biochemistry , vol.44 , pp. 9130-9139
    • Krishnan, N.1    Becker, D.F.2
  • 12
    • 33751088044 scopus 로고    scopus 로고
    • Crystal structures of the DNA-binding domain of Escherichia coli proline utilization a flavoprotein and analysis of the role of Lys9 in DNA recognition
    • JD Larson JL Jenkins JP Schuermann Y Zhou DF Becker JJ Tanner 2006 Crystal structures of the DNA-binding domain of Escherichia coli proline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition Protein Sci 15 2630 2641
    • (2006) Protein Sci , vol.15 , pp. 2630-2641
    • Larson, J.D.1    Jenkins, J.L.2    Schuermann, J.P.3    Zhou, Y.4    Becker, D.F.5    Tanner, J.J.6
  • 13
    • 0037312937 scopus 로고    scopus 로고
    • Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
    • YH Lee S Nadaraia D Gu DF Becker JJ Tanner 2003 Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein Nat Struct Biol 10 109 114
    • (2003) Nat Struct Biol , vol.10 , pp. 109-114
    • Lee, Y.H.1    Nadaraia, S.2    Gu, D.3    Becker, D.F.4    Tanner, J.J.5
  • 14
    • 0028117603 scopus 로고
    • Sequence analysis identifies the proline dehydrogenase and pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein
    • M Ling SW Allen JM Wood 1994 Sequence analysis identifies the proline dehydrogenase and pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein J Mol Biol 245 950 956
    • (1994) J Mol Biol , vol.245 , pp. 950-956
    • Ling, M.1    Allen, S.W.2    Wood, J.M.3
  • 15
    • 0019777101 scopus 로고
    • Purification of the putA gene product
    • R Menzel J Roth 1981 Purification of the putA gene product J Biol Chem 256 9755 9761
    • (1981) J Biol Chem , vol.256 , pp. 9755-9761
    • Menzel, R.1    Roth, J.2
  • 16
    • 0019454689 scopus 로고
    • Regulation of genes for proline utilization in Salmonella typhimurium: Autogenous repression by the putA gene product
    • R Menzel J Roth 1981 Regulation of genes for proline utilization in Salmonella typhimurium: autogenous repression by the putA gene product J Mol Biol 148 21 44
    • (1981) J Mol Biol , vol.148 , pp. 21-44
    • Menzel, R.1    Roth, J.2
  • 17
    • 0030976040 scopus 로고    scopus 로고
    • Regulation of gene expression by repressor localization: Biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive
    • AM Muro-Pastor P Ostrovsky S Maloy 1997 Regulation of gene expression by repressor localization: biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive J Bacteriol 179 2788 2791
    • (1997) J Bacteriol , vol.179 , pp. 2788-2791
    • Muro-Pastor, A.M.1    Ostrovsky, P.2    Maloy, S.3
  • 18
    • 0027294788 scopus 로고
    • PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator
    • P De Ostrovsky Spicer S Maloy 1993 PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator Proc Natl Acad Sci USA 90 4295 4298
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4295-4298
    • De Ostrovsky Spicer, P.1    Maloy, S.2
  • 19
    • 0026024741 scopus 로고
    • Regulation of proline utilization in Salmonella typhimurium: A membrane-associated dehydrogenase binds DNA in vitro
    • P De Ostrovsky Spicer K O'Brian S Maloy 1991 Regulation of proline utilization in Salmonella typhimurium: a membrane-associated dehydrogenase binds DNA in vitro J Bacteriol 173 211 219
    • (1991) J Bacteriol , vol.173 , pp. 211-219
    • De Ostrovsky Spicer, P.1    O'Brian, K.2    Maloy, S.3
  • 21
    • 0018168502 scopus 로고
    • Membrane-bound proline dehydrogenase from Escherichia coli
    • RC Scarpulla RL Soffer 1978 Membrane-bound proline dehydrogenase from Escherichia coli J Biol Chem 253 5997 6001
    • (1978) J Biol Chem , vol.253 , pp. 5997-6001
    • Scarpulla, R.C.1    Soffer, R.L.2
  • 22
    • 4143147468 scopus 로고    scopus 로고
    • Metabolic enzymes and coenzymes in transcription - A direct link between metabolism and transcription?
    • Y Shi Y Shi 2004 Metabolic enzymes and coenzymes in transcription - a direct link between metabolism and transcription? Trends Genet 20 445 452
    • (2004) Trends Genet , vol.20 , pp. 445-452
    • Shi, Y.1    Shi, Y.2
  • 23
    • 0032852996 scopus 로고    scopus 로고
    • Regulation of flavin dehydrogenase compartmentalization: Requirements for PutA-membrane association in Salmonella typhimurium
    • MW Surber S Maloy 1999 Regulation of flavin dehydrogenase compartmentalization: requirements for PutA-membrane association in Salmonella typhimurium Biochim Biophys Acta 1421 5 18
    • (1999) Biochim Biophys Acta , vol.1421 , pp. 5-18
    • Surber, M.W.1    Maloy, S.2
  • 24
    • 0019862229 scopus 로고
    • Genetics of l-proline utilization in Eschericia coli
    • JM Wood 1981 Genetics of l-proline utilization in Eschericia coli J Bacteriol 146 895 901
    • (1981) J Bacteriol , vol.146 , pp. 895-901
    • Wood, J.M.1
  • 25
    • 0005034336 scopus 로고
    • Membrane association of proline dehydrogenase in Escherichia coli is redox dependent
    • J Wood 1987 Membrane association of proline dehydrogenase in Escherichia coli is redox dependent Proc Natl Acad Sci USA 84 373 377
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 373-377
    • Wood, J.1
  • 26
    • 0030924751 scopus 로고    scopus 로고
    • The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide
    • A Zelazny A Seluanov A Cooper E Bibi 1997 The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide Proc Natl Acad Sci USA 94 6025 6029
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6025-6029
    • Zelazny, A.1    Seluanov, A.2    Cooper, A.3    Bibi, E.4
  • 27
    • 5444257841 scopus 로고    scopus 로고
    • Regulation of PutA-membrane associations by flavin adenine dinucleotide reduction
    • W Zhang Y Zhou DF Becker 2004 Regulation of PutA-membrane associations by flavin adenine dinucleotide reduction Biochemistry 43 13165 13174
    • (2004) Biochemistry , vol.43 , pp. 13165-13174
    • Zhang, W.1    Zhou, Y.2    Becker, D.F.3
  • 28
    • 33846185960 scopus 로고    scopus 로고
    • Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2′-OH group in regulating PutA-membrane binding
    • W Zhang M Zhang W Zhu Y Zhou S Wanduragala D Rewinkel JJ Tanner DF Becker 2007 Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2′-OH group in regulating PutA-membrane binding Biochemistry 46 483 491
    • (2007) Biochemistry , vol.46 , pp. 483-491
    • Zhang, W.1    Zhang, M.2    Zhu, W.3    Zhou, Y.4    Wanduragala, S.5    Rewinkel, D.6    Tanner, J.J.7    Becker, D.F.8
  • 29
    • 0037881834 scopus 로고    scopus 로고
    • Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli
    • W Zhu DF Becker 2003 Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli Biochemistry 42 5469 5477
    • (2003) Biochemistry , vol.42 , pp. 5469-5477
    • Zhu, W.1    Becker, D.F.2
  • 30
    • 24944562717 scopus 로고    scopus 로고
    • Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy
    • W Zhu DF Becker 2005 Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy Biochemistry 44 12297 12306
    • (2005) Biochemistry , vol.44 , pp. 12297-12306
    • Zhu, W.1    Becker, D.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.