Control of bacteriophage Mu lysogenic repression

Journal of Molecular Biology

Volumn 353, Issue 1, 2005, Pages 186-195

  Ranquet, Caroline ^a,b,d   Toussaint, Ariane ^a,b   De Jong, Hidde ^c   Maenhaut Michel, Geneviève ^b   Geiselmann, Johannes ^a  

^a UNIV GRENOBLE ALPES   (France)

^b UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^c INRIA RHÔNE ALPES   (France)

^d CEA GRENOBLE   (France)

Author keywords

Lysis lysogeny decision; Modeling; Phage Mu; Proteases; Repressor

Indexed keywords

ENDOPEPTIDASE CLPX; HELICASE; PROTEINASE;

ARTICLE; BACTERIOPHAGE MU; CONTROLLED STUDY; CORRELATION ANALYSIS; GENE INACTIVATION; GENE INDUCTION; GENE REPRESSION; KINETICS; LYSIS; LYSOGENIZATION; MOLECULAR MODEL; NONHUMAN; PHYSIOLOGY; PRIORITY JOURNAL; PROPHAGE; PROTEIN DEGRADATION; PROTEIN STABILITY; PROTEIN TARGETING; QUANTITATIVE ANALYSIS; SIGNAL TRANSDUCTION; SIMULATION;

ENTEROBACTERIA PHAGE MU; ESCHERICHIA COLI;

EID: 25144446275     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.08.015     Document Type: Article

References (42)

1. N. Symonds, A. Toussaint, P.P. Van de, and M. Howe Phage Mu 1987 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
2. A. Toussaint, M.J. Gama, J. Laachouch, G. Maenhaut-Michel, and A. Mhammedi-Alaoui Regulation of bacteriophage Mu transposition Genetica 93 1994 27 39
3. J.L. Vogel, Z.J. Li, M.M. Howe, A. Toussaint, and N.P. Higgins Temperature-sensitive mutations in the bacteriophage Mu c repressor locate a 63-amino-acid DNA-binding domain J. Bacteriol. 173 1991 6568 6577
4. P. Rousseau, M. Betermier, M. Chandler, and R. Alazard Interactions between the repressor and the early operator region of bacteriophage Mu J. Biol. Chem. 271 1996 9739 9745
5. V. Geuskens, A. Mhammedi-Alaoui, L. Desmet, and A. Toussaint Virulence in bacteriophage Mu: a case of trans-dominant proteolysis by the Escherichia coli Clp serine protease EMBO J. 11 1992 5121 5127
6. A. Mhammedi-Alaoui, M. Pato, M.J. Gama, and A. Toussaint A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX protein Mol. Microbiol. 11 1994 1109 1116
7. D.J. Welty, J.M. Jones, and H. Nakai Communication of ClpXP protease hypersensitivity to bacteriophage Mu repressor isoforms J. Mol. Biol. 272 1997 31 41
8. V. Geuskens, J.L. Vogel, R. Grimaud, L. Desmet, N.P. Higgins, and A. Toussaint Frameshift mutations in the bacteriophage Mu repressor gene can confer a trans-dominant virulent phenotype to the phage J. Bacteriol. 173 1991 6578 6585
9. J.E. Laachouch, L. Desmet, V. Geuskens, R. Grimaud, and A. Toussaint Bacteriophage Mu repressor as a target for the Escherichia coli ATP-dependent Clp protease EMBO J. 15 1996 437 444
10. G. Maenhaut-Michel, and J.A. Shapiro The roles of starvation and selective substrates in the emergence of araB-lacZ fusion clones EMBO J. 13 1994 5229 5239
11. S. Lamrani, C. Ranquet, M.J. Gama, H. Nakai, J.A. Shapiro, A. Toussaint, and G. Maenhaut-Michel Starvation-induced Mucts62-mediated coding sequence fusion: a role for ClpXP, Lon, RpoS and Crp Mol. Microbiol. 32 1999 327 343
12. C. Ranquet, J. Geiselmann, and A. Toussaint The tRNA function of SsrA contributes to controlling repression of bacteriophage Mu prophage Proc. Natl Acad. Sci. USA 98 2001 10220 10225
13. D. O'Handley, and H. Nakai Derepression of bacteriophage mu transposition functions by truncated forms of the immunity repressor J. Mol. Biol. 322 2002 311 324
14. D. Weichart, N. Querfurth, M. Dreger, and R. Hengge-Aronis Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli J. Bacteriol. 185 2003 115 125
15. S. Wickner, M.R. Maurizi, and S. Gottesman Posttranslational quality control: folding, refolding, and degrading proteins Science 286 1999 1888 1893
16. U. Jenal, and R. Hengge-Aronis Regulation by proteolysis in bacterial cells Curr. Opin. Microbiol. 6 2003 163 172
17. R.T. Sauer, D.N. Bolon, B.M. Burton, R.E. Burton, J.M. Flynn, and R.A. Grant Sculpting the proteome with AAA(+) proteases and disassembly machines Cell 119 2004 9 18
18. J.M. Flynn, S.B. Neher, Y.I. Kim, R.T. Sauer, and T.A. Baker Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals Mol. Cell 11 2003 671 683
19. S. Gottesman, M.R. Maurizi, and S. Wickner Regulatory subunits of energy-dependent proteases Cell 91 1997 435 438
20. J.L. Vogel, V. Geuskens, L. Desmet, N.P. Higgins, and A. Toussaint C-terminal deletions can suppress temperature-sensitive mutations and change dominance in the phage Mu repressor Genetics 142 1996 661 672
21. H.M. Krause, and N.P. Higgins Positive and negative regulation of the Mu operator by Mu repressor and Escherichia coli integration host factor J. Biol. Chem. 261 1986 3744 3752
22. S.S. Rai, D. O'Handley, and H. Nakai Conformational dynamics of a transposition repressor in modulating DNA binding J. Mol. Biol. 312 2001 311 322
23. T. Schweder, K.H. Lee, O. Lomovskaya, and A. Matin Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease J. Bacteriol. 178 1996 470 476
24. J.A. Kenniston, T.A. Baker, and R.T. Sauer Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing Proc. Natl Acad. Sci. USA 102 2005 1390 1395
25. D. Chandu, and D. Nandi Comparative genomics and functional roles of the ATP-dependent proteases Lon and Clp during cytosolic protein degradation Res. Microbiol. 155 2004 710 719
26. B. Mukhopadhyay, K.R. Marshall-Batty, B.D. Kim, D. O'Handley, and H. Nakai Modulation of phage Mu repressor DNA binding and degradation by distinct determinants in its C-terminal domain Mol. Microbiol. 47 2003 171 182
27. Y.I. Kim, R.E. Burton, B.M. Burton, R.T. Sauer, and T.A. Baker Dynamics of substrate denaturation and translocation by the ClpXP degradation machine Mol. Cell 5 2000 639 648
28. S.K. Singh, R. Grimaud, J.R. Hoskins, S. Wickner, and M.R. Maurizi Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP Proc. Natl Acad. Sci. USA 97 2000 8898 8903
29. D.A. Defenbaugh, and H. Nakai A context-dependent ClpX recognition determinant located at the C terminus of phage Mu repressor J. Biol. Chem. 278 2003 52333 52339
30. K.R. Marshall-Batty, and H. Nakai Trans-targeting of the phage Mu repressor is promoted by conformational changes that expose its ClpX recognition determinant J. Biol. Chem. 278 2003 1612 1617
31. A. Ishihama Modulation of the nucleoid, the transcription apparatus, and the translation machinery in bacteria for stationary phase survival Genes Cells 4 1999 135 143
32. R. Hengge-Aronis Signal transduction and regulatory mechanisms involved in control of the sigma(S) (RpoS) subunit of RNA polymerase Microbiol. Mol. Biol. Rev. 66 2002 373 395
33. Y. Zhou, S. Gottesman, J.R. Hoskins, M.R. Maurizi, and S. Wickner The RssB response regulator directly targets sigma(S) for degradation by ClpXP Genes Dev. 15 2001 627 637
34. S.E. Ades Proteolysis: adaptor, adaptor, catch me a catch Curr. Biol. 14 2004 R924 R926
35. D.N. Bolon, R.A. Grant, T.A. Baker, and R.T. Sauer Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease Mol. Cell 16 2004 343 350
36. M.J. Casadaban Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu J. Mol.Biol. 104 1976 541 555
37. R.W. Simons, F. Houman, and N. Kleckner Improved single and multicopy lac-based cloning vectors for protein and operon fusions Gene 53 1987 85 96
38. E.S. Lennox Transduction of linked genetic characters of the host by bacteriophage P1 Virology 1 1955 190 206
39. H.C. Birnboim, and J. Doly A rapid alkaline extraction procedure for screening recombinant plasmid DNA Nucl. Acids Res. 7 1979 1513 1523
40. T.F.J.F. Maniatis, and J. Sambrook Molecular Cloning: A Laboratory Handbook 1982 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
41. J.A. Kenniston, T.A. Baker, J.M. Fernandez, and R.T. Sauer Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine Cell 114 2003 511 520
42. J. Ortega, H.S. Lee, M.R. Maurizi, and A.C. Steven ClpA and ClpX ATPases bind simultaneously to opposite ends of ClpP peptidase to form active hybrid complexes J. Struct. Biol. 146 2004 217 226