Results 21 to 30 of about 115,119 (230)
Lysine-156 and serine-119 are required for LexA repressor cleavage: a possible mechanism. [PDF]
Proceedings of the National Academy of Sciences, 1987 LexA repressor of Escherichia coli is inactivated in vivo by a specific cleavage reaction requiring activated RecA protein. In vitro, cleavage requires activated RecA at neutral pH and proceeds spontaneously at alkaline pH.
S N Slilaty, John W. Little
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LexA Repressor Forms Stable Dimers in Solution [PDF]
Journal of Biological Chemistry, 2000 Cooperativity in the interactions among proteins subunits and DNA is crucial for DNA recognition. LexA repressor was originally thought to bind DNA as a monomer, with cooperativity leading to tighter binding of the second monomer.
Ronaldo Mohana‐Borges +5 more
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Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy. [PDF]
The EMBO Journal, 1994 The structure of the 84 residue DNA binding domain of the Escherichia coli LexA repressor has been determined from NMR data using distance geometry and restrained molecular dynamics. The assignment of the 1H NMR spectrum of the molecule, derived from 2- and 3-D homonuclear experiments, is also reported.
Rasmus H. Fogh +5 more
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Bacteriophage GIL01 gp7 interacts with host LexA repressor to enhance DNA binding and inhibit RecA-mediated auto-cleavage [PDF]
Nucleic Acids Research, 2015 The SOS response in Eubacteria is a global response to DNA damage and its activation is increasingly associated with the movement of mobile genetic elements.
Nadine Fornelos +5 more
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Interaction of the LexA repressor and the uvrC regulatory region [PDF]
FEBS Letters, 1989 We have studied the in vitro interaction of the LexA repressor protein and the uvrC regulatory region. We find that there is specific binding to two regions, the region we have defined as lexA1 and the lexA2‐lexA3 region. Our findings support the possibility of an inducible regulation for this complex operon.
Thomas F. Stark, R E Moses
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A LexA mutant repressor with a relaxed inter‐domain linker [PDF]
Protein Science, 1998 AbstractThe LexA protein is part of a large family of prokaryotic transcriptional repressors that contain an amino‐terminal DNA binding domain and a carboxy‐terminal dimerization domain. These domains are separated by a linker or hinge region, which is generally considered to be rather flexible and unconstrained. So far, no structure of any of the full‐
Pascale Oertel‐Buchheit +4 more
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A mutant LexA repressor harboring a cleavage motif cysteine‐glycine remains inducible [PDF]
FEBS Letters, 1988 Using site‐directed mutagenesis of the lexA gene we have changed the amino acid Ala‐84 of the LexA repressor for a cysteine. The reason for this change was the striking homology between LexA and UmuD and the comparable size of the two amino acid side chains.
Michèle Granger‐Schnarr +2 more
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LexA protein is a repressor of the colicin E1 gene.
Journal of Biological Chemistry, 1983 LexA protein is a repressor of several chromosomal genes involved in the SOS response in Escherichia coli. In previous experiments, we found that LexA protein may also be a repressor of the colicin E1 gene. We now present evidence that the purified LexA protein strongly repressed the in vitro transcription of the colicin E1 gene. As determined in DNase
Yasuhiko Ebina +4 more
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bioRxivBacteria rely on an arsenal of weapons to challenge their opponents in highly competitive environments. To specifically counter closely related bacteria, specialized weapons with a narrow activity spectrum are deployed, particularly contractile phage ...
Clara Margot Heiman +4 more
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