메뉴 건너뛰기




Volumn 59, Issue 3, 2006, Pages 1025-1036

The C-terminal end of LpxC is required for degradation by the FtsH protease

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID DERIVATIVE; BACTERIAL PROTEIN; FTSH PROTEASE; LPXC PROTEIN; PROTEIN DNAJ; PROTEIN DNAK; PROTEINASE; UNCLASSIFIED DRUG;

EID: 33645085050     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04994.x     Document Type: Article
Times cited : (79)

References (55)
  • 1
    • 0029989855 scopus 로고    scopus 로고
    • FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins
    • Akiyama Y. Kihara A. Tokuda H. Ito K. 1996 FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins J Biol Chem 271 31196 31201
    • (1996) J Biol Chem , vol.271 , pp. 31196-31201
    • Akiyama, Y.1    Kihara, A.2    Tokuda, H.3    Ito, K.4
  • 2
    • 0035087611 scopus 로고    scopus 로고
    • Bacterial cell division protein FtsZ is a specific substrate for the AAA family protease FtsH
    • Anilkumar G. Srinivasan R. Anand SP. Ajitkumar P. 2001 Bacterial cell division protein FtsZ is a specific substrate for the AAA family protease FtsH Microbiology 147 516 517
    • (2001) Microbiology , vol.147 , pp. 516-517
    • Anilkumar, G.1    Srinivasan, R.2    Anand, S.P.3    Ajitkumar, P.4
  • 3
    • 0015451273 scopus 로고
    • Pedigrees of some mutant strains of Escherichia coli K-12
    • Bachmann BJ. 1972 Pedigrees of some mutant strains of Escherichia coli K-12 Bacteriol Rev 36 525 557
    • (1972) Bacteriol Rev , vol.36 , pp. 525-557
    • Bachmann, B.J.1
  • 5
    • 0035937480 scopus 로고    scopus 로고
    • An internal region of the RpoH heat shock transcription factor is critical for rapid degradation by the FtsH protease
    • Bertani D. Oppenheim AB. Narberhaus F. 2001 An internal region of the RpoH heat shock transcription factor is critical for rapid degradation by the FtsH protease FEBS Lett 493 17 20
    • (2001) FEBS Lett , vol.493 , pp. 17-20
    • Bertani, D.1    Oppenheim, A.B.2    Narberhaus, F.3
  • 6
    • 0034231476 scopus 로고    scopus 로고
    • Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
    • Chiba S. Akiyama Y. Mori H. Matsuo E. Ito K. 2000 Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis EMBO Rep 1 47 52
    • (2000) EMBO Rep , vol.1 , pp. 47-52
    • Chiba, S.1    Akiyama, Y.2    Mori, H.3    Matsuo, E.4    Ito, K.5
  • 7
    • 0036720126 scopus 로고    scopus 로고
    • Membrane protein degradation by FtsH can be initiated from either end
    • Chiba S. Akiyama Y. Ito K. 2002 Membrane protein degradation by FtsH can be initiated from either end J Bacteriol 184 4775 4782
    • (2002) J Bacteriol , vol.184 , pp. 4775-4782
    • Chiba, S.1    Akiyama, Y.2    Ito, K.3
  • 9
    • 13444287735 scopus 로고    scopus 로고
    • Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: Insights into the mechanism and inhibitor design
    • Coggins BE. McClerren AL. Jiang L. Li X. Rudolph J. Hindsgaul O. et al. 2005 Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design Biochemistry 44 1114 1126
    • (2005) Biochemistry , vol.44 , pp. 1114-1126
    • Coggins, B.E.1    McClerren, A.L.2    Jiang, L.3    Li, X.4    Rudolph, J.5    Hindsgaul, O.6
  • 10
    • 0034460955 scopus 로고    scopus 로고
    • Sensitive genetic screen for protease activity based on a cyclic AMP signaling cascade in Escherichia coli
    • Dautin N. Karimova G. Ullmann A. Ladant D. 2000 Sensitive genetic screen for protease activity based on a cyclic AMP signaling cascade in Escherichia coli J Bacteriol 182 7060 7066
    • (2000) J Bacteriol , vol.182 , pp. 7060-7066
    • Dautin, N.1    Karimova, G.2    Ullmann, A.3    Ladant, D.4
  • 12
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman S. Roche E. Zhou Y. Sauer RT. 1998 The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system Genes Dev 12 1338 1347
    • (1998) Genes Dev , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 13
    • 8644290874 scopus 로고    scopus 로고
    • A chaperone network controls the heat shock response in E. coli
    • Guisbert E. Herman C. Lu CZ. Gross CA. 2004 A chaperone network controls the heat shock response in E. coli Genes Dev 18 2812 2821
    • (2004) Genes Dev , vol.18 , pp. 2812-2821
    • Guisbert, E.1    Herman, C.2    Lu, C.Z.3    Gross, C.A.4
  • 15
    • 0141789762 scopus 로고    scopus 로고
    • Proteolysis in prokaryotes: Protein quality control and regulatory principles
    • Hengge R. Bukau B. 2003 Proteolysis in prokaryotes: protein quality control and regulatory principles Mol Microbiol 49 1451 1462
    • (2003) Mol Microbiol , vol.49 , pp. 1451-1462
    • Hengge, R.1    Bukau, B.2
  • 17
    • 0031036515 scopus 로고    scopus 로고
    • The HflB protease of Escherichia coli degrades its inhibitor lambda cIII
    • Herman C. Thevenet D. D'Ari R. Bouloc P. 1997 The HflB protease of Escherichia coli degrades its inhibitor lambda cIII J Bacteriol 179 358 363
    • (1997) J Bacteriol , vol.179 , pp. 358-363
    • Herman, C.1    Thevenet, D.2    D'Ari, R.3    Bouloc, P.4
  • 18
    • 2642666491 scopus 로고    scopus 로고
    • Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)
    • Herman C. Thevenet D. Bouloc P. Walker GC. D'Ari R. 1998 Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH) Genes Dev 12 1348 1355
    • (1998) Genes Dev , vol.12 , pp. 1348-1355
    • Herman, C.1    Thevenet, D.2    Bouloc, P.3    Walker, G.C.4    D'Ari, R.5
  • 19
    • 0344211512 scopus 로고    scopus 로고
    • Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH
    • Herman C. Prakash S. Lu CZ. Matouschek A. Gross CA. 2003 Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH Mol Cell 11 659 669
    • (2003) Mol Cell , vol.11 , pp. 659-669
    • Herman, C.1    Prakash, S.2    Lu, C.Z.3    Matouschek, A.4    Gross, C.A.5
  • 20
    • 9744244982 scopus 로고    scopus 로고
    • Zinc hydrolases: The mechanisms of zinc-dependent deacetylases
    • Hernick M. Fierke CA. 2005 Zinc hydrolases: the mechanisms of zinc-dependent deacetylases Arch Biochem Biophys 433 71 84
    • (2005) Arch Biochem Biophys , vol.433 , pp. 71-84
    • Hernick, M.1    Fierke, C.A.2
  • 22
    • 25844525796 scopus 로고    scopus 로고
    • Cellular functions, mechanism of action, and regulation of FtsH protease
    • Ito K. Akiyama Y. 2005 Cellular functions, mechanism of action, and regulation of FtsH protease Annu Rev Microbiol 59 211 231
    • (2005) Annu Rev Microbiol , vol.59 , pp. 211-231
    • Ito, K.1    Akiyama, Y.2
  • 23
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova G. Dautin N. Ladant D. 2005 Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis J Bacteriol 187 2233 2243
    • (2005) J Bacteriol , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 24
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler KC. Waller PRH. Sauer RT. 1996 Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA Science 271 990 993
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.H.2    Sauer, R.T.3
  • 25
    • 0029910627 scopus 로고    scopus 로고
    • A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY
    • Kihara A. Akiyama Y. Ito K. 1996 A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY EMBO J 15 6122 6131
    • (1996) EMBO J , vol.15 , pp. 6122-6131
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 26
    • 0035957955 scopus 로고    scopus 로고
    • Revisiting the lysogenization control of bacteriophage lambda. Identification and characterization of a new host component, HflD
    • Kihara A. Akiyama Y. Ito K. 2001 Revisiting the lysogenization control of bacteriophage lambda. Identification and characterization of a new host component, HflD J Biol Chem 276 13695 13700
    • (2001) J Biol Chem , vol.276 , pp. 13695-13700
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 27
    • 0029787855 scopus 로고    scopus 로고
    • AsmB, a suppressor locus for assembly-defective OmpF mutants of Escherichia coli, is allelic to envA (lpxC)
    • Kloser AW. Laird MW. Misra R. 1996 asmB, a suppressor locus for assembly-defective OmpF mutants of Escherichia coli, is allelic to envA (lpxC) J Bacteriol 178 5138 5143
    • (1996) J Bacteriol , vol.178 , pp. 5138-5143
    • Kloser, A.W.1    Laird, M.W.2    Misra, R.3
  • 28
    • 0031750745 scopus 로고    scopus 로고
    • Modulations in lipid a and phospholipid biosynthesis pathways influence outer membrane protein assembly in Escherichia coli K-12
    • Kloser A. Laird M. Deng M. Misra R. 1998 Modulations in lipid A and phospholipid biosynthesis pathways influence outer membrane protein assembly in Escherichia coli K-12 Mol Microbiol 27 1003 1008
    • (1998) Mol Microbiol , vol.27 , pp. 1003-1008
    • Kloser, A.1    Laird, M.2    Deng, M.3    Misra, R.4
  • 29
    • 0037069332 scopus 로고    scopus 로고
    • The phage lambda CII transcriptional activator carries a C-terminal domain signaling for rapid proteolysis
    • Kobiler O. Koby S. Teff D. Court D. Oppenheim AB. 2002 The phage lambda CII transcriptional activator carries a C-terminal domain signaling for rapid proteolysis Proc Natl Acad Sci USA 99 14964 14969
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14964-14969
    • Kobiler, O.1    Koby, S.2    Teff, D.3    Court, D.4    Oppenheim, A.B.5
  • 30
    • 0031894923 scopus 로고    scopus 로고
    • Lambda Xis degradation in vivo by Lon and FtsH
    • Leffers GG. Jr, Gottesman S. 1998 Lambda Xis degradation in vivo by Lon and FtsH J Bacteriol 180 1573 1577
    • (1998) J Bacteriol , vol.180 , pp. 1573-1577
    • Leffers Jr., G.G.1    Gottesman, S.2
  • 31
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press Cold Spring Harbor, New York
    • Miller JH. 1972 Experiments in Molecular Genetics Cold Spring Harbor, New York Cold Spring Harbor Laboratory Press
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 32
    • 0028584330 scopus 로고
    • An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid a biosynthesis
    • Mohan S. Kelly T. Eveland S. Raetz C. Anderson M. 1994 An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis J Biol Chem 269 32896 32903
    • (1994) J Biol Chem , vol.269 , pp. 32896-32903
    • Mohan, S.1    Kelly, T.2    Eveland, S.3    Raetz, C.4    Anderson, M.5
  • 33
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald AF. Aravind L. Spouge JL. Koonin EV. 1999 AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes Genome Res 9 27 43
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 34
    • 0034050548 scopus 로고    scopus 로고
    • Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli
    • Nishihara K. Kanemori M. Yanagi H. Yura T. 2000 Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli Appl Environ Microbiol 66 884 889
    • (2000) Appl Environ Microbiol , vol.66 , pp. 884-889
    • Nishihara, K.1    Kanemori, M.2    Yanagi, H.3    Yura, T.4
  • 35
    • 0014478053 scopus 로고
    • Mutant of Escherichia coli with anomalous cell division and ability to decrease episomally and chromosomally mediated resistance to ampicillin and several other antibiotics
    • Normark S. Boman HG. Matsson E. 1969 Mutant of Escherichia coli with anomalous cell division and ability to decrease episomally and chromosomally mediated resistance to ampicillin and several other antibiotics J Bacteriol 97 1334 1342
    • (1969) J Bacteriol , vol.97 , pp. 1334-1342
    • Normark, S.1    Boman, H.G.2    Matsson, E.3
  • 36
    • 18944378454 scopus 로고    scopus 로고
    • 32 by a bacterial one-hybrid approach
    • 32 by a bacterial one-hybrid approach J Bacteriol 187 3807 3813
    • (2005) J Bacteriol , vol.187 , pp. 3807-3813
    • Obrist, M.1    Narberhaus, F.2
  • 37
    • 0345523771 scopus 로고    scopus 로고
    • Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid a biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli
    • Ogura T. Inoue K. Tatsuta T. Suzaki T. Karata K. Young K. et al. 1999 Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli Mol Microbiol 31 833 844
    • (1999) Mol Microbiol , vol.31 , pp. 833-844
    • Ogura, T.1    Inoue, K.2    Tatsuta, T.3    Suzaki, T.4    Karata, K.5    Young, K.6
  • 39
    • 0023629563 scopus 로고
    • New and versatile cloning vectors with kanamycin-resistance marker
    • Pridmore RD. 1987 New and versatile cloning vectors with kanamycin-resistance marker Gene 56 309 312
    • (1987) Gene , vol.56 , pp. 309-312
    • Pridmore, R.D.1
  • 41
    • 1642356725 scopus 로고    scopus 로고
    • FtsH exists as an exceptionally large complex containing HflKC in the plasma membrane of Escherichia coli
    • Saikawa N. Akiyama Y. Ito K. 2004 FtsH exists as an exceptionally large complex containing HflKC in the plasma membrane of Escherichia coli J Struct Biol 146 123 129
    • (2004) J Struct Biol , vol.146 , pp. 123-129
    • Saikawa, N.1    Akiyama, Y.2    Ito, K.3
  • 43
    • 8544283778 scopus 로고    scopus 로고
    • Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli
    • Shotland Y. Koby S. Teff D. Mansur N. Oren DA. Tatematsu K. et al. 1997 Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli Mol Microbiol 24 1303 1310
    • (1997) Mol Microbiol , vol.24 , pp. 1303-1310
    • Shotland, Y.1    Koby, S.2    Teff, D.3    Mansur, N.4    Oren, D.A.5    Tatematsu, K.6
  • 44
    • 0029908978 scopus 로고    scopus 로고
    • Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli: The second enzymatic step of lipid a biosynthesis
    • Sorensen PG. Lutkenhaus J. Young K. Eveland SS. Anderson MS. Raetz CRH 1996 Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli: the second enzymatic step of lipid A biosynthesis J Biol Chem 271 25898 25905
    • (1996) J Biol Chem , vol.271 , pp. 25898-25905
    • Sorensen, P.G.1    Lutkenhaus, J.2    Young, K.3    Eveland, S.S.4    Anderson, M.S.5    Raetz, C.R.H.6
  • 46
    • 0021746019 scopus 로고
    • Transcriptional organization within an Escherichia coli cell division gene cluster: Direction of transcription of the cell separation gene envA
    • Sullivan NF. Donachie WD. 1984 Transcriptional organization within an Escherichia coli cell division gene cluster: direction of transcription of the cell separation gene envA J Bacteriol 160 724 732
    • (1984) J Bacteriol , vol.160 , pp. 724-732
    • Sullivan, N.F.1    Donachie, W.D.2
  • 49
    • 0020827719 scopus 로고
    • The dnaK protein modulates the heat-shock response of Escherichia coli
    • Tilly KMN. Zylicz M. Georgopoulos C. 1983 The dnaK protein modulates the heat-shock response of Escherichia coli Cell 34 641 646
    • (1983) Cell , vol.34 , pp. 641-646
    • Tilly, K.M.N.1    Zylicz, M.2    Georgopoulos, C.3
  • 51
    • 0030575933 scopus 로고    scopus 로고
    • Lipid A: Target for antibacterial drugs
    • Vaara M. 1996 Lipid A: target for antibacterial drugs Science 274 939 940
    • (1996) Science , vol.274 , pp. 939-940
    • Vaara, M.1
  • 52
    • 0034047383 scopus 로고    scopus 로고
    • The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation
    • Wehrl W. Niederweis M. Schumann W. 2000 The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation J Bacteriol 182 3870 3873
    • (2000) J Bacteriol , vol.182 , pp. 3870-3873
    • Wehrl, W.1    Niederweis, M.2    Schumann, W.3
  • 54
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C. Vieira J. Messing J. 1985 Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors Gene 33 103 119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 55
    • 0029586501 scopus 로고
    • The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of Lipid a biosynthesis
    • Young K. Silver LL. Bramhill D. Cameron P. Eveland SS. Raetz CRH. et al. 1995 The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of Lipid A biosynthesis J Biol Chem 270 30384 30391
    • (1995) J Biol Chem , vol.270 , pp. 30384-30391
    • Young, K.1    Silver, L.L.2    Bramhill, D.3    Cameron, P.4    Eveland, S.S.5    Raetz, C.R.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.