RecA-dependent cleavage of LexA dimers.
暂无分享,去创建一个
John W. Little | J. W. Little | C. Michalowski | K. C. Giese | Kim C. Giese | Christine B. Michalowski
[1] W. S. Craig. Determination of quaternary structure of an active enzyme using chemical cross-linking with glutaraldehyde. , 1988, Methods in enzymology.
[2] J. Roberts,et al. E. coli recA protein-directed cleavage of phage lambda repressor requires polynucleotide. , 1980, Nature.
[3] J. W. Little,et al. Isolation and characterization of noncleavable (Ind-) mutants of the LexA repressor of Escherichia coli K-12 , 1988, Journal of bacteriology.
[4] R. Woodgate,et al. Intermolecular cleavage by UmuD-like enzymes: identification of residues required for cleavage and substrate specificity. , 1999, Journal of molecular biology.
[5] T. Horii,et al. Regulation of SOS functions: Purification of E. coli LexA protein and determination of its specific site cleaved by the RecA protein , 1981, Cell.
[6] D. Mount,et al. Preferential cleavage of phage lambda repressor monomers by recA protease. , 1981, Nature.
[7] S. Kowalczykowski,et al. In vitro selection of preferred DNA pairing sequences by the Escherichia coli RecA protein. , 1996, Genes & development.
[8] F. Galibert,et al. New recA mutations that dissociate the various RecA protein activities in Escherichia coli provide evidence for an additional role for RecA protein in UV mutagenesis , 1989, Journal of bacteriology.
[9] J. W. Little,et al. The SOS regulatory system: control of its state by the level of RecA protease. , 1983, Journal of molecular biology.
[10] Letter to the Editor: Backbone chemical shift assignments of the LexA catalytic domain in its active conformation , 2005, Journal of biomolecular NMR.
[11] M. Smith,et al. Mutant LexA proteins with an increased rate of in vivo cleavage. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[12] S. Colowick,et al. Methods in Enzymology , Vol , 1966 .
[13] M. Lewis,et al. Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding. , 2000, Cell.
[14] G. Koudelka,et al. The Preferred Substrate for RecA-Mediated Cleavage of Bacteriophage 434 Repressor Is the DNA-Bound Dimer , 2004, Journal of bacteriology.
[15] D. Foguel,et al. LexA Repressor Forms Stable Dimers in Solution , 2000, The Journal of Biological Chemistry.
[16] K. Roland,et al. Cleavage of LexA repressor. , 1994, Methods in enzymology.
[17] M. M. Bradford. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.
[18] J. W. Little. Mechanism of specific LexA cleavage: autodigestion and the role of RecA coprotease. , 1991, Biochimie.
[19] H. Schägger,et al. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. , 1987, Analytical biochemistry.
[20] D. Mount,et al. The SOS regulatory system of Escherichia coli , 1982, Cell.
[21] M. Daune,et al. Large-scale purification, oligomerization equilibria, and specific interaction of the LexA repressor of Escherichia coli. , 1985, Biochemistry.
[22] Jeffrey W. Roberts,et al. E. coli recA protein-directed cleavage of phage λ repressor requires polynucleotide , 1980, Nature.
[23] C. Bell,et al. Structure of a hyper-cleavable monomeric fragment of phage lambda repressor containing the cleavage site region. , 2006, Journal of molecular biology.
[24] G. Weinstock,et al. Binding of the recA protein of Escherichia coli to single- and double-stranded DNA. , 1981, The Journal of biological chemistry.
[25] C. Pabo,et al. Refined 1.8 A crystal structure of the lambda repressor-operator complex. , 1992, Journal of molecular biology.
[26] A. Fersht. Enzyme structure and mechanism , 1977 .
[27] J. W. Little,et al. Mutant LexA proteins with specific defects in autodigestion. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[28] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[29] C. Pace,et al. How to measure and predict the molar absorption coefficient of a protein , 1995, Protein science : a publication of the Protein Society.
[30] J. A. Rupley,et al. Intramolecular cleavage of LexA and phage lambda repressors: dependence of kinetics on repressor concentration, pH, temperature, and solvent. , 1986, Biochemistry.
[31] J. W. Little,et al. Lysine-156 and serine-119 are required for LexA repressor cleavage: a possible mechanism. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[32] Richard A. Pfuetzner,et al. Crystal Structure of LexA A Conformational Switch for Regulation of Self-Cleavage , 2001, Cell.
[33] C. Bell,et al. Structure of a Hyper-cleavable Monomeric Fragment of Phage λ Repressor Containing the Cleavage Site Region , 2006 .
[34] J. W. Little,et al. Robustness of a gene regulatory circuit , 1999, The EMBO journal.
[35] G. K. Ackers,et al. Energetics of subunit dimerization in bacteriophage lambda cI repressor: linkage to protons, temperature, and KCl. , 1991, Biochemistry.
[36] Jeffrey W. Roberts,et al. Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication. , 1990, Journal of molecular biology.
[37] L. Beamer,et al. Refined 1.8 p crystal structure of the ? repressor-operator complex*1 , 1992 .
[38] J. W. Little,et al. Autodigestion and RecA-dependent cleavage of Ind- mutant LexA proteins. , 1989, Journal of molecular biology.
[39] R. Sauer,et al. Mutations inBacteriophage XRepressor ThatPrevent RecA-Mediated Cleavage , 1985 .
[40] H. Echols,et al. Repressor cleavage as a prophage induction mechanism: hypersensitivity of a mutant lambda cI protein to recA-mediated proteolysis. , 1981, Journal of molecular biology.
[41] E. G. Frank,et al. Structure of the UmuD′ protein and its regulation in response to DNA damage , 1996, Nature.
[42] M. Cox,et al. C-terminal Deletions of the Escherichia coli RecA Protein , 2003, The Journal of Biological Chemistry.
[43] N. Guex,et al. SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling , 1997, Electrophoresis.
[44] R. Scheuermann,et al. UmuD mutagenesis protein of Escherichia coli: overproduction, purification, and cleavage by RecA. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[45] J. W. Little,et al. Autodigestion of lexA and phage lambda repressors. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[46] R. Sauer,et al. Lambda repressor inactivation: properties of purified ind- proteins in the autodigestion and RecA-mediated cleavage reactions. , 1986, Journal of molecular biology.
[47] R. Sauer,et al. Lambda repressor mutants that are better substrates for RecA-mediated cleavage. , 1989, Journal of molecular biology.
[48] A. Engel,et al. Characterization of complexes between recA protein and duplex DNA by electron microscopy. , 1982, Journal of molecular biology.
[49] A. Hochschild,et al. Specificity determinants for the interaction of lambda repressor and P22 repressor dimers. , 1994, Genes & development.
[50] E. Egelman,et al. The LexA repressor binds within the deep helical groove of the activated RecA filament. , 1993, Journal of molecular biology.
[51] E. Egelman,et al. Complexes of RecA with LexA and RecX differentiate between active and inactive RecA nucleoprotein filaments. , 2003, Journal of molecular biology.
[52] J. A. Rupley,et al. In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage. , 1992, Journal of molecular biology.
[53] F. Harmon,et al. Interaction of Escherichia coli RecA Protein with LexA Repressor , 1996, The Journal of Biological Chemistry.
[54] M. Lewis,et al. Crystal Structure of the λ Repressor C-Terminal Domain Provides a Model for Cooperative Operator Binding , 2000, Cell.
[55] G. Walker,et al. Differential cleavage of LexA and UmuD mediated by recA Pro67 mutants: implications for common LexA and UmuD binding sites on RecA. , 1998, Journal of molecular biology.