Proteolysis in Bacterial Regulatory Circuits

Annual Review of Cell and Developmental Biology

Volumn 19, Issue , 2003, Pages 565-587

  Gottesman, Susan ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Chaperone; Clp; FtsH; Hsl; Lon

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL ENZYME; PROTEINASE;

AMINO TERMINAL SEQUENCE; BACILLUS SUBTILIS; CARBOXY TERMINAL SEQUENCE; CAULOBACTER CRESCENTUS; CELL CYCLE; CONFERENCE PAPER; CYTOPLASM; ENERGY TRANSFER; ESCHERICHIA COLI; EUKARYOTE; GENE TRANSLOCATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; SIGNAL TRANSDUCTION;

ADAPTOR PROTEINS, VESICULAR TRANSPORT; ADENOSINE TRIPHOSPHATASES; BACTERIA; CELL CYCLE; EUKARYOTIC CELLS; FEEDBACK, BIOCHEMICAL; PEPTIDE HYDROLASES; PROTEIN STRUCTURE, TERTIARY;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); CAULOBACTER VIBRIOIDES; ESCHERICHIA COLI; EUKARYOTA; NEGIBACTERIA; POSIBACTERIA;

EID: 0344824655     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.19.110701.153228     Document Type: Conference Paper

References (141)

1. Akiyama Y, Kihara A, Mori H, Ogura T, Ito K. 1998. Roles of the periplasmic domain of Escherichia coli FtsH (HflB) in protein interactions and activity modulation. J. Biol. Chem. 273:22362-33
2. 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: 31196-201
3. E dependent extracytoplasmic stress response. Genes Dev. 16:2156-68
4. Banuett F, Hoyt MA, McFarlane L, Echols H, Herskowitz I. 1986. hflB, a new Escherichia coli locus regulating lysogeny and the level of bacteriophage lambda CII protein. J. Mol. Biol. 187:213-24
5. Belfort M, Wulff DL. 1973. Genetic and biochemical investigation of the Eschericha coli mutant hfl-1 which is lysogenized at high frequency by bacteriophage lambda. J. Bacteriol. 115:299-306
6. Beuron F, Maurizi MR, Belnap DM, Kocsis E, Booy FP, et al. 1998. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J. Struct. Biol. 123:248-59
7. Bi E, Lutkenhaus J. 1990. Analysis of ftsZ mutations that confer resistance to the cell division inhibitor SulA (SfiA). J. Bacteriol. 172: 5602-9
8. Biran D, Gur E, Gollan L, Ron EZ. 2000. Control of methionine biosynthesis in Escherichia coli by proteolysis. Mol. Microbiol. 37:1436-43
9. Bochtler M, Hartmann C, Song HK, Bourenkov GP Bartunik HD, Huber R. 2000. The structure of HslU and the ATP-dependent protease HslU-HslV. Nature 403:800-5
10. Braun BC, Glickman M, Kraft R, Dahlmann B, Kloetzel P-M, et al. 1999. The base of the proteasome regulatory particle exhibits chaperone-like activity. Nat. Cell Biol. 1:221-26
11. Brown AJ, Sun L, Feramisco JD, Brown MS, Goldstein JL. 2002. Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism. Mol. Cell 10:237-45
12. Brown MS, Ye J, Rawson RB, Goldstein JL. 2000. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100:391-98
13. Charette M, Henderson GW, Markovitz A. 1981. ATP hydrolysis-dependent activity of the lon(capR) protein of E. coli K12. Proc. Natl. Acad. Sci. USA 78:4728-32
14. Chastanet A, Prudhomme M, Claverys J-P, Msadek T. 2001. Regulation of Streptococcus pneumoniae clp genes and their role in competence development and stress survival. J. Bacteriol. 183:7295-307
15. Chung CH, Goldberg AL. 1981. The product of the Ion (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Proc. Natl. Acad. Sci. USA 78:4931-35
16. Corydon TJ, Bross P, Holst HU, Neves S, Kristiansen K, et al. 1998. A human homologue of Escherichia coli ClpP caseinolytic protease: recombinant expression, intracellular processing and subcellular localization. Biochem. J. 331:309-16
17. Cutting S, Anderson M, Lysenko E, Page A, Tomoyasu T, et al. 1997. SpoVM, a small protein essential to development in Bacillus subtilis, interacts with the ATP-dependent protease FtsH. J. Bacteriol. 179:5534-42
18. Domian IJ, Quon KC, Shapiro L. 1997. Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle. Cell 90:415-24
19. Doronina VA, Murray NE. 2001. The proteolytic control of restriction activity in Escherichia coli K-12. Mol. Microbiol. 39:416-28
20. Dougan DA, Reid BG, Horwich AL, Bukau B. 2002. ClpS, a substrate modulator of the ClpAP machine. Mol. Cell 9:673-83
21. Dubnau D. 1999. DNA uptake in bacteria. Annu. Rev. Microbiol. 53:217-44
22. Flynn JM, Neher SB, Kim Y-I, Sauer RT, Baker TA. 2003. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 11:671-83
23. Frank EG, Ennis DG, Gonzalez M, Levine AS, Woodgate R. 1996. Regulation of SOS mutagenesis by proteolysis. Proc. Natl. Acad. Sci. USA 93:10291-96
24. Fukui T, Eguchi T, Atomi H, Imanaka T. 2002. A membrane-bound archael Lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteins. J. Bacteriol. 184:3689-98
25. George J, Castellazzi M, Buttin G. 1975. Prophage induction and cell division in E. coli. III. Mutations sfiA and sfiB restore division in tif and Ion strains and permit the mutator properties of tif. Mol. Gen. Genet. 140: 309-32
26. Gerth U, Kruger K, Derre I, Msadek T, Hecker M. 1998. Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance. Mol. Microbiol. 28:787-802
27. Goldberg AL, John ACS. 1976. Intracellular protein degradation in mammalian and bacterial cells. Annu. Rev. Biochem. 45:747-803
28. Gonciarz-Swiatek M, Wawrzynow A, Um SJ, Learn BA, McMacken R, et al. 1999. Recognition, targeting, and hydrolysis of the lambda O replication protein by the ClpP/ClpX protease. J. Biol Chem. 274:13999-4005
29. Gonzalez M, Frank EG, Levine AS, Woodgate R. 1998. Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis. Genes Dev. 12:3889-99
30. Gonzalez M, Rasulova F, Maurizi MR, Woodgate R. 2000. Subunit-specific degradation of the UmuD/D′ heterodimer by the ClpXP protease: the role of trans recognition in UmuD' stability. EMBO J. 19:5251-58
31. Gottesman S. 1996. Roles for energy-dependent proteases in regulatory cascades. In Regulation of Gene Expression in Escherichia coli, ed. ECC Lin, AS Lynch, pp. 503-19. Austin, TX: Landes
32. Gottesman S, Clark WP, de Crecy-Lagard V, Maurizi MR. 1993. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 268:22618-26
33. Gottesman S, Roche E, Zhou Y-N, Sauer RT. 1998. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the S srA-tagging system. Genes Dev. 12:1338-47
34. Gottesman S, Wickner S, Maurizi MR. 1997. Protein quality control: triage by chaperones and proteases. Genes Dev. 11:815-23
35. Grimaud R, Kessel M, Beuron F, Stevens AC, Maurizi MR. 1998. Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J. Biol. Chem. 273:12476-81
36. Grunenfelder B, Rummel G, Vohradsky J, Roder D, Langen H, Jenal U. 2001. Proteomic analysis of the bacterial cell cycle. Proc. Natl. Acad. Sci. USA 98:4681-86
37. + chaperone, ClpA. J. Biol. Chem. 277:46753-62
38. Guo F, Maurizi MR, Esser L, Xia D. 2002b. Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J. Biol. Chem. 277:46743-52
39. S (RpoS) subunit of RNA polymerase. Microbiol. Mol. Biol. Rev. 66:373-95
40. Herman C, Thévenet D, Bouloc P, Walker GC, D'Ari R. 1998. Degradation of carboxyterminal-tagged cytoplsmic proteins by the Escherichia coli protease HflB (FtsH). Genes Dev. 12:1348-55
41. Herman C, Thévenet D, D'Ari R, Bouloc P. 1997. The HflB protease of Escherichia coli degrades its inhibitor λcIII. J. Bacteriol. 179:358-63
42. Herman C, Thévenet D, D'Ari R, Bouloc P. 1995. Degradation of σ32, the heat shock regulator in Escherichia coli, is governed by HflB. Proc. Natl. Acad. Sci. USA 92:3516-20
43. Hershko A, Ciechanover A. 1998. The ubiquitin system. Annu. Rev. Biochem. 67:425-79
44. Hilliard JJ, Maurizi MR, Simon LD. 1998. Isolation and characterization of the phage T4 PinA protein, an inhibitor of the ATP-dependent Lon protease of Escherichia coli. J. Biol. Chem. 273:518-23
45. Hoskins JR, Kim SY, Wickner S. 2000a. Substrate recognition by the ClpA chaperone component of ClpAP protease. J. Biol. Chem. 275:35361-67
46. Hoskins JR, Singh SK, Maurizi MR, Wickner S. 2000b. Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP. Proc. Natl. Acad. Sci. USA 97:8892-97
47. Hoskins JR, Yanagihira K, Mizuuchi K, Wickner S. 2002. ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence. Proc. Natl. Acad. Sci. USA 99:11037-42
48. Hughes KT, Mathee K. 1998. The anti-sigma factors. Annu. Rev. Microbiol. 52:231-86
49. Huisman O, D'Ari R, Gottesman S. 1984. Cell division control in Escherichia coli: Specific induction of the SOS SfiA protein is sufficient to block septation. Proc. Natl. Acad. Sci. USA 81:4490-94
50. Hwang BJ, Park WJ, Chung CH, Goldberg AL. 1987. Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La. Proc. Natl. Acad. Sci. USA 84:5550-54
51. Ishii Y, Amano F. 2001. Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine. Biochem. J. 358:473-80
52. Ishikawa T, Beuron F, Kessel M, Wickner S, Maurizi MR, Steven AC. 2001. Translocation pathway of protein substrates in ClpAP protease. Proc. Natl. Acad. Sci. USA 98:4328-33
53. Jenal U, Fuchs T. 1998. An essential protease involved in bacterial cell-cycle control. EMBO J. 17:5658-69
54. Jenal U, Stephens C. 2002. The Caulobacter cell cycle: timing, spatial organization and checkpoints. Curr. Opin. Microbiol. 5:558-63
55. Jones JM, Welty DJ, Nakai H. 1998. Versatile action of Escherichia coli ClpXP as a protease or molecular chaperone for bacteriophage Mu transposition. J. Biol. Chem. 273:459-65
56. Judson HF. 1979. The Eighth Day of Creation: The Makers of the Revolution in Biology. New York: Simon & Schuster
57. E, RseA. Genes Dev. 16:2147-55
58. Kang SG, Ortega J, Singh SK, Wang N, Huang NN, et al. 2002. Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP. J. Biol. Chem. 277:21095-102
59. Katayama-Fujimura Y, Gottesman S, Maurizi MR. 1987. A multiple-component ATP-dependent protease from Escherichia coli. J. Biol. Chem. 262:4477-85
60. Keiler KC, Waller PRH, Sauer RT. 1996. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271:990-93
61. Kessel M, Maurizi MR, Kirn B, Kocsis E, Trus BL, et al. 1995. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26S proteasome. J. Mol. Biol. 250:587-94
62. Kessel M, Wu W-F, Gottesman S, Kocsis E, Steven AC, Maurizi MR. 1996. Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. FEBS Lett. 398: 274-78
63. Kihara A, Akiyama Y, Ito K. 1995. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc. Natl. Acad. Sci. USA 92:4532-36
64. 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. 15:6122-31
65. Kihara A, Akiyama Y, Ito K. 1997. Host regulation of lysogenic decision in bacteriophage λ: transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA). Proc. Natl. Acad. Sci. USA 94:5544-49
66. Kihara A, Akiyama Y, Ito K. 1999. Dislocation of membrane proteins in FtsH-mediated proteolysis. EMBO J. 18:2970-81
67. Kim YI, Levchenko I, Fraczkowska K, Woodruff RV, Sauer RT, Baker TA. 2001. Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase. Nat. Struct. Biol. 8:230-33
68. S proteolysis in Escherichia coli. Mol. Microbiol. 40:1381-90
69. Kruger E, Zuhlke D, Witt E, Ludwig H, Hecker M. 2001. Clp-mediated proteolysis in gram-positive bacteria is autoregulated by the stability of a repressor. EMBO J. 20:852-63
70. Krzywda S, Brzozowski AM, Verma C, Karata K, Ogura T, Wilkinson AJ. 2002. The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 Å resolution. Structure 10:1073-83
71. Kuroda A, Nomura K, Ohtomo R, Kato J, Ikeda T, et al. 2001. Role of inorganic polyphosphate promoting ribosomal protein degradation by the Lon protease in E. coli. Science 293:705-8
72. Lee C, Schwartz MP, Prakash S, Iwakura M, Matouschek A. 2001. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7:627-37
73. Leffers GG Jr, Gottesman S. 1998. Lambda Xis degradation in vivo by Lon and FtsH. J. Bacteriol. 180:1573-77
74. Levchenko I, Luo L, Baker TA. 1995. Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev. 9:2399-408
75. Levchenko I, Seidel M, Sauer RT, Baker TA. 2000. A specificity-enhancing factor for the ClpXP degradation machine. Science 289: 2345-56
76. Levchenko I, Yamauchi M, Baker TA. 1997. ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Genes Dev. 11:1561-72
77. Little JW, Edmiston SH, Pacelli LZ, Mount DW. 1980. Cleavage of the Escherichia coli lexA protein by the recA protease. Proc. Natl. Acad. Sci. USA 77:3225-29
78. Lupas A, Flanagan JM, Tamura T, Baumeister W 1997. Self- compartmentalizing proteases. Trends Biochem. Sci. 22:399-404
79. Lutkenhaus JF. 1983. Coupling of DNA replication and cell divison: sulB is an allele of ftsZ. J. Bacteriol. 154:1339-46
80. Makovets S, Doronina VA, Murray NE. 1999. Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes. Proc. Natl. Acad. Sci. USA 96:9757-62
81. Maurizi MR. 1998. Biochemical properties and biological functions of ATP-dependent proteases in bacterial cells. Adv. Mol. Cell Biol. 27:1-41
82. Maurizi MR, Clark WP, Kim S-H, Gottesman S. 1990. ClpP represents a unique family of serine proteases. J. Biol. Chem. 265:12546-52
83. Miller CG. 1996. Protein degradation and proteolytic modification. In Escherichia coli and Salmonella: Cellular and Molecular Biology, ed. FC Neidhardt, R Curtiss III, JL Ingraham, ECC Lin, KB Low, et al., pp. 938-54. Washington, DC: Am. Soc. Microbiol. 2nd ed.
84. Missiakas D, Schwager F, Betton JM, Georgopoulos C, Raina S. 1996. Identification and characterization of HslV HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J. 15:6899-909
85. Mizusawa S, Gottesman S. 1983. Protein degradation in Escherichia coli: the Ion gene controls the stability of the SulA protein. Proc. Natl. Acad. cid. USA 80:358-62
86. Motohashi K, Watanabe Y, Yohda M, Yoshida M. 1999. Heat-inactivated proteins are rescued by the DnaK J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. USA 96:7184-89
87. Nakano S, Zheng G, Nakano MM, Zuber P. 2002. Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilis. J. Bacteriol. 184:3664-70
88. Neher SB, Flynn JM, Sauer RT, Baker TA. 2003. Latent ClpX-recognition signals ensure LexA degradation after DNA damage. Genes Dev. 17:1084-89
89. Niwa H, Tsuchiya D, Makyio H, Yoshida M, Morikawa K. 2002. Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8. Structure 10:1415-23
90. Nohmi T, Battista JR, Dodson LA, Walker GC. 1988. RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation. Proc. Natl. Acad. Sci. USA 85:1816-20
91. Ogura T, Inoue K, Tatsuta T, Suzaki T, Karata 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. 31:833-44
92. + superfamily ATPases: common structure-diverse function. Genes Cells 6:575-97
93. Ortega J, Lee HS, Maurizi MR, Steven AC. 2002. Alternating translocation of protein substrates from both ends of ClpXP protease. EMBO J. 21:4938-49
94. Ortega J, Singh SK, Ishikawa T, Maurizi MR, Steven AC. 2000. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell 6:1515-21
95. Persuh M, Mandic-Mulec I, Dubnau D. 2002. A MecA paralog, YpbH, binds ClpC, affecting both competence and sporulation. J. Bacteriol. 184:2310-13
96. Persuh M, Turgay K, Mandic-Mulec I, Dubnau D. 1999. The N-and C-terminal domains of MecA recognize different partners in the competence molecular switch. Mol. Microbiol 33:886-94
97. Petersen C. 1990. Escherichia coli ribosomal protein L10 is rapidly degraded when synthesized in excess of ribosomal protein L7/L12. J. Bacteriol. 172:431-36
98. Potocka I, Thein M, Osteras M, Jenal U, Alley MRK. 2002. Degradation of a Caulobacter soluble cytoplasmic chemoreceptor is ClpX dependent. J. Bacteriol. 184:6635-41
99. S turnover in Escherichia coli. Mol. Microbiol. 45:1701-13
100. Raivio TL, Silhavy TJ. 2001. Periplasmic stress and ECF sigma factors. Annu. Rev. Microbiol. 55:591-624
101. Reichardt LF. 1975. Control of bacteriophage lambda repressor synthesis after phage infection: the role of the N, cII, cIII and cro products. J. Mol. Biol. 93:267-88
102. Roberts JW, Roberts CW. 1975. Proteolytic cleavage of bacteriophage lambda repressor in induction. Proc. Natl Acad. Sci. USA 72: 147-51
103. Rohrwild M, Coux O, Huang H-C, Moerschell RP, Yoo SJ, et al. 1996. HslV-HslU: a novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc. Natl. Acad. Sci. USA 93:5808-13
104. Rudner DZ, Fawcett P, Losick R. 1999. A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors. Proc. Natl. Acad. Sci. USA 96:14765-70
105. Sanchez Y, Parsell DA, Taulien J, Vogel JL, Craig EA, Lindquist S. 1993. Genetic evidence for a functional relationship between Hsp104 and Hsp70. J. Bacteriol. 175:6484-91
106. G. J. Bacteriol. 176:6528-37
107. S) by ClpXP protease. J. Bacteriol. 178:470-76
108. Serrano M, Hovel S, Moran CPJ, Henriques AO, Volker U. 2001. Forespore-specific transcription of the lonB gene during sporulation in Bacillus subtilis. J. Bacteriol. 183:2995-3003
109. Shinagawa H, Iwasaki H, Kato T, Nakata A. 1988. RecA protein-dependent cleavage of UmuD protein and SOS mutagenesis. Proc. Natl. Acad. Sci. USA 85:1806-10
110. Shotland Y, Koby S, Teff D, Mansur N, Oren DA, et al. 1997. Proteolysis of the phage λ cII regulatory protein by FtsH (HflB) of Escherichia coli. Mol. Microbiol. 24:1303-10
111. Singh SK, Grimaud R, Hoskins JR, Wickner S, Maurizi MR. 2000. Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP. Proc. Natl. Acad. Sci. USA 97:8898-903
112. Sousa MC, Kessler BM, Overkleeft HS, McKay DB. 2002. Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU. J. Mol. Biol. 318:779-85
113. Stahlberg H, Kutejova E, Suda K, Wolpensinger B, Lustig A, et al. 1999. Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits. Proc. Natl. Acad. Sci. USA 96:6787-90
114. 32. Genes Dev. 4:2202-9
115. Sutton MD, Smith BT, Godoy VG, Walker GC. 2000. The SOS response: recent insights into umuDC-dependent mutagenesis and DNA damage tolerance. Annu. Rev. Genet. 34:479-97
116. 32. EMBO J. 14:2551-60
117. Tsai J-W, Alley MRK. 2001. Proteolysis of the Caulobacter McpA chemoreceptor is cell cycle regulated by a ClpX-dependent pathway. J. Bacteriol. 183:5001-7
118. Turgay K, Hahn J, Burghoorn J, Dubnau D. 1998. Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor. EMBO J. 17:6730-38
119. Turgay K, Hamoen LW, Venema G, Dubnau D. 1997. Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis. Genes Dev. 11:119-28
120. Ueda K, Yamamoto Y, Ogawa K, Abo T, Inokuchi H, Aiba H. 2002. Bacterial SsrA system plays a role in coping with unwanted translational readthrough caused by suppressor tRNAs. Genes Cells 7:509-19
121. Van Melderen L, Gottesman S. 1999. Substrate sequestration by a proteolytically inactive Ion mutant. Proc. Natl. Acad. Sci. USA 96:6064-71
122. Van Melderen L, Thi MHD, Lecchi P, Gottesman S, Couturier M, Maurizi MR. 1996. ATP-dependent degradation of CcdA by Lon protease: effects of secondary structure and heterologous subunit interactions. J. Biol. Chem. 271:27730-38
123. Varshavsky A. 1992. The N-end rule. Cell 69: 725-35
124. + ATPase. Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer. Chem. Biol. 9:1237-45
125. Wang J, Hartling JA, Flanagan JM. 1997. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell 91:447-56
126. Wang J, Song JJ, Seong IS, Franklin MC, Kamtekar S, et al. 2001. Nucleotide-dependent conformational changes in a protease-associated ATPase HslU. Structure 9:1107-16
127. Wawrzynow A, Wojtkowiak D, Marzsalek J, Banecki B, Jonsen M, et al. 1995. The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14:1867-77
128. 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
129. Wegrzyn G, Paltowicz A, Taylor K. 1992. Stability of coliphage λ DNA replication initiator, the λO protein. J. Mol. Biol. 226:675-80
130. Weichart D, Querfurth N, Dreger M, Hengge-Aronis R. 2003. Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. J. Bacteriol. 185:115-25
131. Weisberg RA, Gottesman ME. 1971. The stability of Int and Xis functions. In The Bacteriophage Lambda, ed. AD Hershey, pp. 489-500. Cold Spring Harbor, NY: Cold Spring Harbor Lab.
132. Wickner S, Gottesman S, Skowyra D, Hoskins J, McKenney K, Maurizi MR. 1994. A molecular chaperone, CIpA, functions like DnaK and DnaJ. Proc. Natl. Acad. Sci. USA 91:12218-22
133. Wickner S, Maurizi MR, Gottesman S. 1999. Posttranslational quality control: folding, refolding, and degrading proteins. Science 286: 1888-93
134. P22 growth in Escherichia coli. J. Bacteriol. 181:2148-57
135. Withey JH, Friedman DI. 2003. A salvage pathway for protein synthesis: tmRNA and transtranslation. Annu. Rev. Microbiol. 57:101-23
136. Wojtkowiak D, Georgopoulos C, Zylicz M. 1993. ClpX, a new specificity component of the ATP-dependent Escherichia coli Clp protease, is potentially involved in λ DNA replication. J. Biol. Chem. 268:22609-17
137. Wright R, Stephens C, Zweiger C, Shapiro L, Alley MRK. 1996. Caulobacter Lon protease has a critical role in cell cycle control of DNA methylation. Genes Dev. 10:1532-42
138. Yura T, Kanemori M, Morita MT. 2000. The heat shock response: regulation and function. In Bacterial Stress Responses, ed. G Storz, R Hengge-Aronis, pp. 3-18. Washington, DC: ASM Press
139. 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. 9:906-11
140. S for degradation by ClpXP. Genes Dev. 15:627-37
141. Zolkiewski M. 1999. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J. Biol. Chem. 274:28083-86