메뉴 건너뛰기




Volumn 28, Issue 12, 2009, Pages 1732-1744

Modification of PATase by L/F-transferase generates a ClpS-dependent N-end rule substrate in Escherichia coli

Author keywords

ClpS; LFTR; N degron; N end rule pathway; Substrate binding

Indexed keywords

ADENOSINE TRIPHOSPHATE; ESCHERICHIA COLI PROTEIN; LEUCYLPHENYLALANYL TRNA PROTEIN TRANSFERASE; PROTEIN CLPAP; PROTEIN CLPS; PUTRESCINE AMINOTRANSFERASE; TRANSFER RNA; UNCLASSIFIED DRUG; AMINOACYLTRANSFERASE; AMINOTRANSFERASE; CARRIER PROTEIN; CLPA PROTEASE, E COLI; CLPP PROTEASE, E COLI; CLPS PROTEIN, E COLI; DIPEPTIDE; DPS PROTEIN, E COLI; ENDOPEPTIDASE CLP; LEUCYLTRANSFERASE; LIGAND; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN;

EID: 67649552963     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2009.134     Document Type: Article
Times cited : (76)

References (36)
  • 1
    • 0027083350 scopus 로고
    • A novel DNAbinding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron M, Link AJ, Furlong D, Kolter R (1992) A novel DNAbinding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev 6: 2646-2654
    • (1992) Genes Dev , vol.6 , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 3
    • 1942537173 scopus 로고    scopus 로고
    • Catanzariti AM, Soboleva TA, Jans DA, Board Baker RT (2004) An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci 13: 1331-1339
    • Catanzariti AM, Soboleva TA, Jans DA, Board PG, Baker RT (2004) An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci 13: 1331-1339
  • 4
    • 10244243805 scopus 로고    scopus 로고
    • DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus
    • Ceci P, Cellai S, Falvo E, Rivetti C, Rossi GL, Chiancone E (2004) DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus. Nucleic Acids Res 32: 5935-5944
    • (2004) Nucleic Acids Res , vol.32 , pp. 5935-5944
    • Ceci, P.1    Cellai, S.2    Falvo, E.3    Rivetti, C.4    Rossi, G.L.5    Chiancone, E.6
  • 5
    • 0036810483 scopus 로고    scopus 로고
    • Protein folding and degradation in bacteria: To degrade or not to degrade? That is the question
    • Dougan DA, Mogk A, Bukau B (2002a) Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question. Cell Mol Life Sci 59: 1607-1616
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1607-1616
    • Dougan, D.A.1    Mogk, A.2    Bukau, B.3
  • 6
    • 0036210995 scopus 로고    scopus 로고
    • ClpS, a substrate modulator of the ClpAP machine
    • Dougan DA, Reid BG, Horwich AL, Bukau B (2002b) ClpS, a substrate modulator of the ClpAP machine. Mol Cell 9: 673-683
    • (2002) Mol Cell , vol.9 , pp. 673-683
    • Dougan, D.A.1    Reid, B.G.2    Horwich, A.L.3    Bukau, B.4
  • 9
    • 4444377383 scopus 로고    scopus 로고
    • Modulating substrate choice: The SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation
    • Flynn JM, Levchenko I, Sauer RT, Baker TA (2004) Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation. Genes Dev 18: 2292-2301
    • (2004) Genes Dev , vol.18 , pp. 2292-2301
    • Flynn, J.M.1    Levchenko, I.2    Sauer, R.T.3    Baker, T.A.4
  • 10
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn JM, Neher SB, Kim YI, Sauer RT, Baker TA (2003) Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol Cell 11: 671-683
    • (2003) Mol Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 12
    • 0029155041 scopus 로고
    • Decrease in cell viability due to the accumulation of spermidine in spermidine acetyltransferase-deficient mutant of Escherichia coli
    • Fukuchi J, Kashiwagi K, Yamagishi M, Ishihama A, Igarashi K (1995) Decrease in cell viability due to the accumulation of spermidine in spermidine acetyltransferase-deficient mutant of Escherichia coli. J Biol Chem 270: 18831-18835
    • (1995) J Biol Chem , vol.270 , pp. 18831-18835
    • Fukuchi, J.1    Kashiwagi, K.2    Yamagishi, M.3    Ishihama, A.4    Igarashi, K.5
  • 13
    • 0034596991 scopus 로고    scopus 로고
    • Subunitspecific degradation of the UmuD/D' heterodimer by the ClpXP protease: The role of trans recognition in UmuD' stability
    • Gonzalez M, Rasulova F, Maurizi MR, Woodgate R (2000) Subunitspecific degradation of the UmuD/D' heterodimer by the ClpXP protease: the role of trans recognition in UmuD' stability. EMBO J 19: 5251-5258
    • (2000) EMBO J , vol.19 , pp. 5251-5258
    • Gonzalez, M.1    Rasulova, F.2    Maurizi, M.R.3    Woodgate, R.4
  • 14
    • 0038690474 scopus 로고    scopus 로고
    • Regulation by proteolysis in bacterial cells
    • Jenal U, Hengge-Aronis R (2003) Regulation by proteolysis in bacterial cells. Curr Opin Microbiol 6: 163-172
    • (2003) Curr Opin Microbiol , vol.6 , pp. 163-172
    • Jenal, U.1    Hengge-Aronis, R.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0037287864 scopus 로고    scopus 로고
    • Bioinformatic analysis of ClpS, a protein module involved in prokaryotic and eukaryotic protein degradation
    • Lupas AN, Koretke KK (2003) Bioinformatic analysis of ClpS, a protein module involved in prokaryotic and eukaryotic protein degradation. J Struct Biol 141: 77-83
    • (2003) J Struct Biol , vol.141 , pp. 77-83
    • Lupas, A.N.1    Koretke, K.K.2
  • 17
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps
    • Martinez A, Kolter R (1997) Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. J Bacteriol 179: 5188-5194
    • (1997) J Bacteriol , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 18
    • 33947713897 scopus 로고    scopus 로고
    • The N-end rule pathway for regulated proteolysis: Prokaryotic and eukaryotic strategies
    • Mogk A, Schmidt R, Bukau B (2007) The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol 17: 165-172
    • (2007) Trends Cell Biol , vol.17 , pp. 165-172
    • Mogk, A.1    Schmidt, R.2    Bukau, B.3
  • 19
    • 3042662444 scopus 로고    scopus 로고
    • Dps protects cells against multiple stresses during stationary phase
    • Nair S, Finkel SE (2004) Dps protects cells against multiple stresses during stationary phase. J Bacteriol 186: 4192-4198
    • (2004) J Bacteriol , vol.186 , pp. 4192-4198
    • Nair, S.1    Finkel, S.E.2
  • 20
    • 0035912183 scopus 로고    scopus 로고
    • Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability
    • Rao H, Uhlmann F, Nasmyth K, Varshavsky A (2001) Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability. Nature 410: 955-959
    • (2001) Nature , vol.410 , pp. 955-959
    • Rao, H.1    Uhlmann, F.2    Nasmyth, K.3    Varshavsky, A.4
  • 21
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • Ravid T, Hochstrasser M (2008) Diversity of degradation signals in the ubiquitin-proteasome system. Nat Rev Mol Cell Biol 9: 679-690
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 22
  • 23
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 24
    • 0027255191 scopus 로고
    • The N-end rule in Escherichia coli: Cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat
    • Shrader TE, Tobias JW, Varshavsky A (1993) The N-end rule in Escherichia coli: cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat. J Bacteriol 175: 4364-4374
    • (1993) J Bacteriol , vol.175 , pp. 4364-4374
    • Shrader, T.E.1    Tobias, J.W.2    Varshavsky, A.3
  • 26
    • 0016367645 scopus 로고
    • A mutant of Escherichia coli defective in leucyl, phenylalanyl-tRNA-protein transferase
    • Soffer RL, Savage M (1974) A mutant of Escherichia coli defective in leucyl, phenylalanyl-tRNA-protein transferase. Proc Natl Acad Sci USA 71: 1004-1007
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1004-1007
    • Soffer, R.L.1    Savage, M.2
  • 27
    • 33845706511 scopus 로고    scopus 로고
    • Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog
    • Suto K, Shimizu Y,Watanabe K, Ueda T, Fukai S, Nureki O, Tomita K (2006) Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog. EMBO J 25: 5942-5950
    • (2006) EMBO J , vol.25 , pp. 5942-5950
    • Suto, K.1    Shimizu, Y.2    Watanabe, K.3    Ueda, T.4    Fukai, S.5    Nureki, O.6    Tomita, K.7
  • 28
    • 35548974677 scopus 로고    scopus 로고
    • The mammalian N-end rule pathway: New insights into its components and physiological roles
    • Tasaki T, Kwon YT (2007) The mammalian N-end rule pathway: new insights into its components and physiological roles. Trends Biochem Sci 32: 520-528
    • (2007) Trends Biochem Sci , vol.32 , pp. 520-528
    • Tasaki, T.1    Kwon, Y.T.2
  • 30
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky A (1996) The N-end rule: functions, mysteries, uses. Proc Natl Acad Sci USA 93: 12142-12149
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 31
    • 20444404618 scopus 로고    scopus 로고
    • Regulated protein degradation
    • Varshavsky A (2005) Regulated protein degradation. Trends Biochem Sci 30: 283-286
    • (2005) Trends Biochem Sci , vol.30 , pp. 283-286
    • Varshavsky, A.1
  • 32
    • 33847226240 scopus 로고    scopus 로고
    • ClpS modulates but is not essential for bacterial N-end rule degradation
    • Wang KH, Sauer RT, Baker TA (2007) ClpS modulates but is not essential for bacterial N-end rule degradation. Genes Dev 21: 403-408
    • (2007) Genes Dev , vol.21 , pp. 403-408
    • Wang, K.H.1    Sauer, R.T.2    Baker, T.A.3
  • 33
    • 35348938968 scopus 로고    scopus 로고
    • Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase
    • Watanabe K, Toh Y, Suto K, Shimizu Y, Oka N, Wada T, Tomita K (2007) Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase. Nature 449: 867-871
    • (2007) Nature , vol.449 , pp. 867-871
    • Watanabe, K.1    Toh, Y.2    Suto, K.3    Shimizu, Y.4    Oka, N.5    Wada, T.6    Tomita, K.7
  • 34
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • Weber-Ban EU, Reid BG, Miranker AD, Horwich AL (1999) Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 401: 90-93
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 35
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner S, Maurizi MR, Gottesman S (1999) Posttranslational quality control: folding, refolding, and degrading proteins. Science 286: 1888-1893
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 36
    • 0036896886 scopus 로고    scopus 로고
    • Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA
    • Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA (2002) Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Nat Struct Biol 9: 906-911
    • (2002) Nat Struct Biol , vol.9 , pp. 906-911
    • Zeth, K.1    Ravelli, R.B.2    Paal, K.3    Cusack, S.4    Bukau, B.5    Dougan, D.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.