Results 191 to 200 of about 9,038 (230)

LexA repressor induces operator-dependent DNA bending

Journal of Molecular Biology, 1988
LexA, the repressor of the SOS system in Escherichia coli induces a substantial DNA bending upon interaction with the operator of the caa gene, which codes for the bacterial toxin colicin A. Analysis by gel electrophoresis of a family of DNA fragments of identical length, but bearing the caa operator at different positions, shows that DNA bending ...
R, Lloubès, M, Granger-Schnarr, C, Lazdunski, M, Schnarr   +3 more
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DNA binding properties of the LexA repressor

Biochimie, 1991
The LexA repressor from Escherichia coli negatively regulates the transcription of about 20 different genes upon binding with variable affinity to single-, double- or even triple-operators as in the case of the recN gene. Binding of LexA to multiple operators is cooperative if the spacing between these operators is favorable.
M, Schnarr, P, Oertel-Buchheit, M, Kazmaier, M, Granger-Schnarr   +3 more
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A model for the LexA repressor DNA complex

Proteins: Structure, Function, and Bioinformatics, 1995
AbstractA structural model for the interaction of the LexA repressor DNA binding domain (DBD) with operator DNA is derived by means of Monte Carlo docking. Protein–DNA complexes were generated by docking the LexA repressor DBD NMR solution structure onto both rigid and bent B‐DNA structures while giving energy bonuses for contacts in agreement with ...
Knegtel, R.M.A., Fogh, R.H., Ottleben, G., Ruterjans, H., Dumoulin, P., Schnarr, M., Boelens, R., Kaptein, R.   +7 more
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Genetic analysis of the LexA repressor: Isolation and characterization of LexA(Def) mutant proteins

Molecular and General Genetics MGG, 1990
We report the isolation of LexA mutant proteins with impaired repressor function. These mutant proteins were obtained by transforming a LexA-deficient recA-lacZ indicator strain with a randomly mutagenized plasmid harbouring the lexA gene and subsequent selection on MacConkey-lactose indicator plates.
P, Oertel-Buchheit, R M, Lamerichs, M, Schnarr, M, Granger-Schnarr   +3 more
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Binding of Escherichia coli lexA repressor to the RecA operator

Journal of Molecular Recognition, 1996
Equilibrium binding of Escherichia coli LexA repressor to the recA operator was studied by the polyacrylamide gel mobility shift assay as a function of solution conditions. In the presence of NaCl at 20 degrees C, there was a significant salt dependence in binding to the recA operator, typical for protein-nucleic acid interactions with some ...
S L, Shaner, E S, Gaissarian
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Model of a LexA Repressor Dimer Bound torecA Operator

Journal of Biomolecular Structure and Dynamics, 2000
A complete three dimensional model (RCSB000408; PDB code 1qaa) for the LexA repressor dimer bound to the recA operator site consistent with relevant biochemical and biophysical data for the repressor is proposed. A model of interaction of the N-terminal operator binding domain 1-72 with the operator was available.
R, Chattopadhyaya, K, Ghosh, V M, Namboodiri   +2 more
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Improved Model of a LexA Repressor Dimer Bound torecAOperator

Journal of Biomolecular Structure and Dynamics, 2004
A complete three dimensional model for the LexA repressor dimer bound to the recA operator site consistent with relevant biochemical and biophysical data for the repressor was proposed from our laboratory when no crystal structure of LexA was available. Subsequently, the crystal structures of four LexA mutants Delta(1-67) S119A, S119A, G85D and Delta(1-
Rajagopal, Chattopadhyaya, Atasi, Pal
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Intramolecular cleavage of lexA and phage .lambda. repressors: dependence of kinetics on repressor concentration, pH, temperature, and solvent

Biochemistry, 1986
LexA repressor of Escherichia coli and phage lambda repressor are inactivated in vivo and in vitro by specific cleavage of an Ala-Gly peptide bond in reactions requiring RecA protein. At mildly alkaline pH, the in vitro cleavage reaction also proceeds spontaneously, suggesting that peptide bond hydrolysis is an activity of the repressors rather than of
S N, Slilaty, J A, Rupley, J W, Little
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LexA and λ Cl repressors as enzymes: Specific cleavage in an intermolecular reaction

Cell, 1993
During the SOS response, LexA repressor is inactivated by specific cleavage. Although cleavage requires RecA protein in vivo, RecA acts indirectly as a coprotease by stimulating an inherent self-cleavage activity of LexA. In lambda lysogens, cleavage of lambda Cl repressor in a similar but far slower reaction results in prophage induction.
B, Kim, J W, Little
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The protein HU can displace the LexA repressor from its DNA‐binding sites

Molecular Microbiology, 1994
SummaryThe major bacterial histone‐like protein HU is a small, basic, dimeric protein composed of two closely related subunits. HU is involved in several processes in the bacterial cell such as the initiation of replication, transposition, gene inversion and cell division.
O, Preobrajenskaya, A, Boullard, F, Boubrik, M, Schnarr, J, Rouvière-Yaniv   +4 more
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