Structure of a Hyper-cleavable Monomeric Fragment of Phage λ Repressor Containing the Cleavage Site Region

Journal of Molecular Biology

Volumn 362, Issue 3, 2006, Pages 479-489

  Ndjonka, Dieudonné ^a   Bell, Charles E ^a  

^a THE OHIO STATE UNIVERSITY COLLEGE OF MEDICINE   (United States)

Author keywords

bacteriophage lambda; DNA repair; lambda repressor; LexA; RecA protein

Indexed keywords

DNA; RECA PROTEIN;

ARTICLE; BACTERIOPHAGE LAMBDA; CARBOXY TERMINAL SEQUENCE; CHEMICAL BOND; CONFORMATIONAL TRANSITION; DNA DAMAGE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME MECHANISM; GENE DELETION; GENE DISRUPTION; GENE INDUCTION; GENE REPRESSION; LYSIS; LYSOGENIZATION; MOLECULAR INTERACTION; OLIGOMERIZATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STABILITY; STRUCTURE ANALYSIS;

ENTEROBACTERIA PHAGE LAMBDA;

EID: 33748103187     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.07.026     Document Type: Article

References (29)

1. Ptashne M. A Genetic Switch. 3rd edit. (2004), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
2. Roberts J.W., and Roberts C.W. Proteolytic cleavage of bacteriophage lambda repressor in induction. Proc. Natl Acad. Sci. USA 72 (1975) 147-151
3. Little J.W. Autodigestion of lexA and phage lambda repressors. Proc. Natl Acad. Sci. USA 81 (1984) 1375-1379
4. Cohen S., Knoll B.J., Little J.W., and Mount D.W. Preferential cleavage of phage lambda repressor monomers by recA protease. Nature 294 (1981) 182-184
5. Craig N.L., and Roberts J.W. E. coli recA protein-directed cleavage of phage lambda repressor requires polynucleotide. Nature 283 (1980) 26-30
6. Phizicky E.M., and Roberts J.W. Kinetics of RecA protein-directed inactivation of repressors of phage lambda and phage P22. J. Mol. Biol. 139 (1980) 319-328
7. Shinagawa H., Iwasaki H., Kato T., and Nakata A. RecA protein-dependent cleavage of UmuD protein and SOS mutagenesis. Proc. Natl Acad. Sci. USA 85 (1988) 1806-1810
8. Horii T., Ogawa T., Nakatani T., Hase T., Matsubara H., and Ogawa H. Regulation of SOS functions: purification of E. coli LexA protein and determination of its specific site cleaved by the RecA protein. Cell 27 (1981) 515-522
9. Pabo C.O., Sauer R.T., Sturtevant J.M., and Ptashne M. The lambda repressor contains two domains. Proc. Natl Acad. Sci. USA 76 (1979) 1608-1612
10. Slilaty S.N., and Little J.W. Lysine-156 and serine-119 are required for LexA repressor cleavage: a possible mechanism. Proc. Natl Acad. Sci. USA 84 (1987) 3987-3991
11. Peat T.S., Frank E.G., McDonald J.P., Levine A.S., Woodgate R., and Hendrickson W.A. Structure of the UmuD' protein and its regulation in response to DNA damage. Nature 380 (1996) 727-730
12. Luo Y., Pfuetzner R.A., Mosimann S., Paetzel M., Frey E.A., Cherney M., et al. Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Cell 106 (2001) 585-594
13. Bell C.E., Frescura P., Hochschild A., and Lewis M. Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding. Cell 101 (2000) 801-811
14. Sauer R.T., Ross M.J., and Ptashne M. Cleavage of the lambda and P22 repressors by recA protein. J. Biol. Chem. 257 (1982) 4458-4462
15. Roland K.L., Smith M.H., Rupley J.A., and Little J.W. In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage. J. Mol. Biol. 228 (1992) 395-408
16. Pabo C.O., and Lewis M. The operator-binding domain of lambda repressor: structure and DNA recognition. Nature 298 (1982) 443-447
17. Jordan S.R., and Pabo C.O. Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions. Science 242 (1988) 893-899
18. Bell C.E., and Lewis M. Crystal structure of the lambda repressor C-terminal domain octamer. J. Mol. Biol. 314 (2001) 1127-1136
19. Gimble F.S., and Sauer R.T. Lambda repressor mutants that are better substrates for RecA-mediated cleavage. J. Mol. Biol. 206 (1989) 29-39
20. Whipple F.W., Kuldell N.H., Cheatham L.A., and Hochschild A. Specificity determinants for the interaction of lambda repressor and P22 repressor dimers. Genes Dev. 8 (1994) 1212-1223
21. Lin L.L., and Little J.W. Autodigestion and RecA-dependent cleavage of Ind- mutant LexA proteins. J. Mol. Biol. 210 (1989) 439-452
22. Pinkett H.W., Shearwin K.E., Stayrook S., Dodd I.B., Burr T., Hochschild A., et al. The structural basis of cooperative regulation at an alternate genetic switch. Mol. Cell 21 (2006) 605-615
23. De J., and Sauer R.T. P22 c2 repressor. Domain structure and function. J. Biol. Chem. 258 (1983) 10536-10542
24. Gimble F.S., and Sauer R.T. Lambda repressor inactivation: properties of purified ind- proteins in the autodigestion and RecA-mediated cleavage reactions. J. Mol. Biol. 192 (1986) 39-47
25. Gimble F.S., and Sauer R.T. Mutations in bacteriophage lambda repressor that prevent RecA-mediated cleavage. J. Bacteriol. 162 (1985) 147-154
26. Yu X., and Egelman E.H. The LexA repressor binds within the deep helical groove of the activated RecA filament. J. Mol. Biol. 231 (1993) 29-40
27. Xing X., and Bell C.E. Crystal structures of Escherichia coli RecA in a compressed helical filament. J. Mol. Biol. 342 (2004) 1471-1485
28. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallog. sect. D 54 (1998) 905-921
29. Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119