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Volumn 13, Issue 1, 2013, Pages

Stabilized homoserine o-succinyltransferases (MetA) or L-methionine partially recovers the growth defect in Escherichia coli lacking ATP-dependent proteases or the DnaK chaperone

Author keywords

ATP dependent proteases; DnaK chaperone; Escherichia coli; Growth rate; Homoserine o succinyltransferase (MetA); Thermostability

Indexed keywords

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; HOMOSERINE SUCCINYLTRANSFERASE; METHIONINE; PROTEIN DNAK;

EID: 84880862940     PISSN: None     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-13-179     Document Type: Article
Times cited : (8)

References (35)
  • 1
    • 84859482204 scopus 로고    scopus 로고
    • Methionine biosynthesis in Escherichia coli and corynebacterium glutamicum
    • Berlin, Heidelberg: Springer Wendisch VF 23908659
    • Methionine biosynthesis in Escherichia coli and corynebacterium glutamicum. Figge RM, Amino acid biosynthesis-pathways, regulation and metabolic engineering Berlin, Heidelberg: Springer, Wendisch VF, 2006 164 189 23908659
    • (2006) Amino Acid Biosynthesis - Pathways, Regulation and Metabolic Engineering , pp. 164-189
    • Figge, R.M.1
  • 3
    • 0033607238 scopus 로고    scopus 로고
    • Enzyme-catalyzed acylation of homoserine: Mechanistic characterization of the Escherichia coli metA-encoded homoserine transsuccinylase
    • DOI 10.1021/bi991710o
    • Enzyme-catalyzed acylation of homoserine: Mechanistic characterization of the Escherichia coli metA-encoded homoserine transsuccinylase. Born TL, Blanchard JS, Biochemistry 1999 38 14416 14423 10.1021/bi991710o 10572016 (Pubitemid 29513858)
    • (1999) Biochemistry , vol.38 , Issue.43 , pp. 14416-14423
    • Born, T.L.1    Blanchard, J.S.2
  • 4
    • 0014203841 scopus 로고
    • Enzymatic synthesis of homocysteine or methionine directly from O-succinylhomoserine
    • 10.1016/0005-2744(67)90158-1 5340123
    • Enzymatic synthesis of homocysteine or methionine directly from O-succinylhomoserine. Flavin M, Slaughter C, Biochim Biophys Acta 1967 132 400 405 10.1016/0005-2744(67)90158-1 5340123
    • (1967) Biochim Biophys Acta , vol.132 , pp. 400-405
    • Flavin, M.1    Slaughter, C.2
  • 6
    • 0033770817 scopus 로고    scopus 로고
    • Control of methionine biosynthesis in Escherichia coli by proteolysis
    • 10.1046/j.1365-2958.2000.02097.x 10998174
    • Control of methionine biosynthesis in Escherichia coli by proteolysis. Biran D, Gur E, Gollan L, Ron EZ, Mol Microbiol 2000 37 1436 1443 10.1046/j.1365-2958.2000.02097.x 10998174
    • (2000) Mol Microbiol , vol.37 , pp. 1436-1443
    • Biran, D.1    Gur, E.2    Gollan, L.3    Ron, E.Z.4
  • 7
    • 17644423441 scopus 로고    scopus 로고
    • Polyphosphate kinase protects Salmonella enterica from weak organic acid stress
    • DOI 10.1128/JB.187.9.3088-3099.2005
    • Polyphosphate kinase protects Salmonella enterica from weak organic acid stress. Price-Carter M, Fazzio TG, Vallbona EI, Roth JR, J Bacteriol 2005 187 3088 3099 10.1128/JB.187.9.3088-3099.2005 15838036 (Pubitemid 40571602)
    • (2005) Journal of Bacteriology , vol.187 , Issue.9 , pp. 3088-3099
    • Price-Carter, M.1    Fazzio, T.G.2    Vallbona, E.I.3    Roth, J.R.4
  • 8
    • 0015102446 scopus 로고
    • Growth rate of Escherichia coli at elevated temperatures: Limitation by methionine
    • 4939758
    • Growth rate of Escherichia coli at elevated temperatures: limitation by methionine. Ron EZ, Davis BD, J Bacteriol 1971 107 391 396 4939758
    • (1971) J Bacteriol , vol.107 , pp. 391-396
    • Ron, E.Z.1    Davis, B.D.2
  • 9
    • 0036887272 scopus 로고    scopus 로고
    • In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperatures
    • DOI 10.1046/j.1365-2958.2002.03257.x
    • In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperature. Gur E, Biran D, Gazit E, Ron EZ, Mol Microbiol 2002 46 1391 1397 10.1046/j.1365-2958.2002.03257.x 12453224 (Pubitemid 36961272)
    • (2002) Molecular Microbiology , vol.46 , Issue.5 , pp. 1391-1397
    • Gur, E.1    Biran, D.2    Gazit, E.3    Ron, E.Z.4
  • 11
    • 57449100055 scopus 로고    scopus 로고
    • Improved thermostability and acetic acid tolerance of Escherichia coli via directed evolution of homoserine o-succinyltransferase
    • 10.1128/AEM.00654-08 18978085
    • Improved thermostability and acetic acid tolerance of Escherichia coli via directed evolution of homoserine o-succinyltransferase. Mordukhova EA, Lee H-S, Pan J-G, Appl Environ Microbiol 2008 74 7660 7668 10.1128/AEM.00654-08 18978085
    • (2008) Appl Environ Microbiol , vol.74 , pp. 7660-7668
    • Mordukhova, E.A.1    Lee, H.-S.2    Pan, J.-G.3
  • 12
    • 0035424955 scopus 로고    scopus 로고
    • Engineering proteins for thermostability: The use of sequence alignments versus rational design and directed evolution
    • DOI 10.1016/S0958-1669(00)00229-9
    • Engineering proteins for thermostability: the use of sequence alignment versus rational design and directed evolution. Lehmann M, Wyss M, Curr Opin Biotechnol 2001 12 371 375 10.1016/S0958-1669(00)00229-9 11551465 (Pubitemid 32718790)
    • (2001) Current Opinion in Biotechnology , vol.12 , Issue.4 , pp. 371-375
    • Lehmann, M.1    Wyss, M.2
  • 13
    • 23144461249 scopus 로고    scopus 로고
    • I-Mutant2.0: Predicting stability changes upon mutation from the protein sequence or structure
    • DOI 10.1093/nar/gki375
    • I-Mutant2.0: predicting stability changes upon mutation from the protein sequence or structure. Capriotti E, Fariselli P, Casadio R, Nucleic Acids Res 2005 33 306 310 10.1093/nar/gki375 (Pubitemid 44529932)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISSUE.
    • Capriotti, E.1    Fariselli, P.2    Casadio, R.3
  • 14
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. Mogk A, Tomoyasu T, Goloubinoff P, Rüdiger S, Röder D, Langen H, Bukau B, EMBO J 1999 18 6934 6949 10.1093/emboj/18.24.6934 10601016 (Pubitemid 30000447)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6    Bukau, B.7
  • 15
    • 0023123175 scopus 로고
    • Escherichia coli dnaK null mutants are inviable at high temperature
    • Escherichia coli dnaK null mutant are inviable at high temperature. Paek K-H, Walker GC, J Bacteriol 1987 169 283 290 3025174 (Pubitemid 17228720)
    • (1987) Journal of Bacteriology , vol.169 , Issue.1 , pp. 283-290
    • Paek, K.-H.1    Walker, G.C.2
  • 16
    • 0030613795 scopus 로고    scopus 로고
    • 32 and abnormal proteins in Escherichia coli
    • Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of σ§ssup§32§esup§ and abnormal proteins in Escherichia coli. Kanemori M, Nishihara K, Yanagi H, Yura T, J Bacteriol 1997 179 7219 7225 9393683 (Pubitemid 27509956)
    • (1997) Journal of Bacteriology , vol.179 , Issue.23 , pp. 7219-7225
    • Kanemori, M.1    Nishihara, K.2    Yanagi, H.3    Yura, T.4
  • 17
    • 71749092092 scopus 로고    scopus 로고
    • Temperature-dependent proteolysis as a control element in Escherichia coli metabolism
    • 10.1016/j.resmic.2009.08.015 19770038
    • Temperature-dependent proteolysis as a control element in Escherichia coli metabolism. Katz C, Rasouly A, Gur E, Shenhar Y, Biran D, Ron EZ, Res Microbiol 2009 160 684 686 10.1016/j.resmic.2009.08.015 19770038
    • (2009) Res Microbiol , vol.160 , pp. 684-686
    • Katz, C.1    Rasouly, A.2    Gur, E.3    Shenhar, Y.4    Biran, D.5    Ron, E.Z.6
  • 19
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Factors enhancing protein thermostability. Kumar S, Tsai C-J, Nissinov R, Protein Eng 2000 13 179 191 10.1093/protein/13.3.179 10775659 (Pubitemid 30237592)
    • (2000) Protein Engineering , vol.13 , Issue.3 , pp. 179-191
    • Kumar, S.1    Tsai, C.-J.2    Nussinov, R.3
  • 20
    • 4444330121 scopus 로고    scopus 로고
    • Structural basis of protein kinetic stability: Resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward β-sheet structure
    • DOI 10.1021/bi0491898
    • Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward β-sheet structure. Manning M, Colon W, Biochemistry 2004 43 11248 11254 10.1021/bi0491898 15366934 (Pubitemid 39180368)
    • (2004) Biochemistry , vol.43 , Issue.35 , pp. 11248-11254
    • Manning, M.1    Colon, W.2
  • 21
    • 77951977004 scopus 로고    scopus 로고
    • Protein kinetic stability
    • 10.1016/j.bpc.2010.02.004 20199841
    • Protein kinetic stability. Sanchez-Ruiz JM, Biophys Chem 2010 148 1 15 10.1016/j.bpc.2010.02.004 20199841
    • (2010) Biophys Chem , vol.148 , pp. 1-15
    • Sanchez-Ruiz, J.M.1
  • 23
    • 0024672180 scopus 로고
    • Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism
    • 2651398
    • Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism. Bukau B, Walker GC, J Bacteriol 1989 171 2337 2346 2651398
    • (1989) J Bacteriol , vol.171 , pp. 2337-2346
    • Bukau, B.1    Walker, G.C.2
  • 24
    • 0041817974 scopus 로고    scopus 로고
    • Minimization of cavity size ensures protein stability and folding: Structures of Phe46-replaced bovine pancreatic RNase A
    • DOI 10.1021/bi034499w
    • Minimization of cavity size ensures protein stability and folding: structures of Phe46-replaced bovine pancreatic RNase A. Kadonosono T, Chatani E, Hayashi R, Moriyama H, Ueki T, Biochemistry 2003 42 10651 10658 10.1021/bi034499w 12962489 (Pubitemid 37102104)
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10651-10658
    • Kadonosono, T.1    Chatani, E.2    Hayashi, R.3    Moriyama, H.4    Ueki, T.5
  • 26
    • 0037200114 scopus 로고    scopus 로고
    • A procedure for detection and quantitation of cavity volumes in proteins: Application to measure the strength of the hydrophobic driving force in protein folding
    • DOI 10.1074/jbc.M201373200
    • A procedure for detection and quantification of cavity volumes in proteins. Chakravarty S, Bhinge A, Varadarajan R, J Biol Chem 2002 277 31345 31353 10.1074/jbc.M201373200 12070144 (Pubitemid 34968933)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.35 , pp. 31345-31353
    • Chakravarty, S.1    Bhinge, A.2    Varadarajan, R.3
  • 28
    • 78650003023 scopus 로고    scopus 로고
    • Genes that move the window of viability of life: Lessons from bacteria thriving at the cold extreme: Mesophiles can be turned into extremophiles by substituting essential genes
    • 10.1002/bies.201000101 21072830
    • Genes that move the window of viability of life: lessons from bacteria thriving at the cold extreme: mesophiles can be turned into extremophiles by substituting essential genes. De Lorenzo V, Bioessays 2011 33 38 42 10.1002/bies.201000101 21072830
    • (2011) Bioessays , vol.33 , pp. 38-42
    • De Lorenzo, V.1
  • 29
    • 0033042865 scopus 로고    scopus 로고
    • Evolutionary adaptation to temperature. VII. Extension of the upper thermal limit of Escherichia coli
    • Evolutionary adaptation to temperature VII. Extension of the upper thermal limit of Escherichia coli. Mongold JA, Bennett AF, Lenski RE, Evolution 1999 53 386 394 10.2307/2640775 (Pubitemid 29239711)
    • (1999) Evolution , vol.53 , Issue.2 , pp. 386-394
    • Mongold, J.A.1    Bennett, A.F.2    Lenski, R.E.3
  • 30
    • 22544461606 scopus 로고    scopus 로고
    • Phenotypic alteration and target gene identification using combinatorial libraries of zinc finger proteins in prokaryotic cells
    • DOI 10.1128/JB.187.15.5496-5499.2005
    • Phenotypic alteration and target gene identification using combinatorial libraries of zinc finger proteins in prokaryotic cells. Park K-S, Jang Y-S, Lee H, Kim J-S, J Bacteriol 2005 187 5496 5499 10.1128/JB.187.15.5496-5499.2005 16030245 (Pubitemid 41022969)
    • (2005) Journal of Bacteriology , vol.187 , Issue.15 , pp. 5496-5499
    • Park, K.-S.1    Jang, Y.-S.2    Lee, H.3    Kim, J.-S.4
  • 33
    • 44849138934 scopus 로고    scopus 로고
    • Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
    • DOI 10.1038/nsmb.1425, PII NSMB1425
    • Protein disaggregation by the AAA + chaperone ClpB involves partial threading of looped polypeptide segments. Haslberger T, Zdanowicz A, Brand I, Kirstein J, Turgay K, Mogk A, Bukau B, Nat Struct Mol Biol 2008 15 641 650 10.1038/nsmb.1425 18488042 (Pubitemid 351799133)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.6 , pp. 641-650
    • Haslberger, T.1    Zdanowicz, A.2    Brand, I.3    Kirstein, J.4    Turgay, K.5    Mogk, A.6    Bukau, B.7
  • 34
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • DOI 10.1046/j.1365-2958.2001.02383.x
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Tomoyasu T, Mogk A, Langen H, Goloubinoff P, Bukau B, Mol Microbiol 2001 40 397 413 10.1046/j.1365-2958.2001.02383.x 11309122 (Pubitemid 32391634)
    • (2001) Molecular Microbiology , vol.40 , Issue.2 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5
  • 35
    • 58249090831 scopus 로고    scopus 로고
    • Studying tmRNA-mediated surveillance and nonstop mRNA decay
    • 19161851, KRIBB Innovation Grant
    • Studying tmRNA-mediated surveillance and nonstop mRNA decay. Sundermeier T, Ge Z, Richards J, Dulebohn D, Karzai AW, Methods Enzymol 2008 447 329 358 19161851
    • (2008) Methods Enzymol , vol.447 , pp. 329-358
    • Sundermeier, T.1    Ge, Z.2    Richards, J.3    Dulebohn, D.4    Karzai, A.W.5


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