Results 211 to 220 of about 115,119 (230)

Chapter 772 – Repressor LexA

, 2013
J. W. Little
semanticscholar   +3 more sources

Control of the LexA regulon by pH: evidence for a reversible inactivation of the LexA repressor during the growth cycle of Escherichia coli

Molecular Microbiology, 1994
SummaryThe LexA repressor controls the expression of several genes, including lexA, recA, and sfiA, which are induced when exponentially growing bacteria are exposed to DNA‐damaging agents, Induction of this so‐called SOS response takes place while LexA is cleaved in a reaction that requires the RecA protein and damaged DNA.
A. Dri, P. Moreau
semanticscholar   +4 more sources

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.
Manfred Schnarr, Michèle Granger-Schnarr, Pascale Oertel-Buchheit, M. Kazmaier   +3 more
openaire   +3 more sources

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 ...
Heinz Rüterjans, Rolf Boelens, Manfred Schnarr, R. M. A. Knegtel, G. Ottleben, Robert Kaptein, Pascal Dumoulin, Rasmus H. Fogh   +7 more
openaire   +4 more sources

[20] Cleavage of LexA repressor

1994
Publisher Summary This chapter examines cleavage of LexA repressor. In normally growing cells, about 20 SOS genes are turned off by the LexA repressor. On inducing treatments, LexA undergoes specific proteolytic cleavage; cleavage inactivates LexA and leads to derepression of the SOS genes. This specific cleavage reaction is of biological interest as
John W. Little, Baek Kim, Margaret H. Smith, Lih Ling Lin, Kenneth L. Roland, Steve N. Slilaty   +5 more
openaire   +3 more sources

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.
Michèle Granger-Schnarr, Manfred Schnarr, R.M.J.N. Lamerichs, Pascale Oertel-Buchheit   +3 more
openaire   +3 more sources

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 ...
Michèle Granger-Schnarr, Claude Lazdunski, Manfred Schnarr, Roland Lloubès   +3 more
openaire   +3 more sources

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 ...
Sandra L. Shaner, Elisabeth S. Gaissarian   +1 more
openaire   +3 more sources

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.
Rajagopal Chattopadhyaya, Kaushik Ghosh, V. M. Haridasan Namboodiri   +2 more
openaire   +3 more sources

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
openaire   +3 more sources