Results 101 to 110 of about 4,885 (120)

P. mirabilis RecA protein catalyses cleavage of E. coli LexA protein and the λ repressor in vitro

Molecular and General Genetics MGG, 1984
The cloned recA+ gene of proteus mirabilis substitutes for a defective RecA protein in Escherichia coli recA- mutants, and restores recombination, repair and phage induction functions to near normal levels. In a previous report, we described the purification and characterisation of the recombination activities of the P.
S C, West, J W, Little
openaire   +2 more sources

Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper: a circular dichroism and mutagenesis study

Biochemistry, 1991
An increasing number of eukaryotic transcription factors interacting specifically with DNA comprise a dimerization motif called the "leucine zipper". These leucine zipper proteins form homodimers and/or heterodimers with another protein containing a leucine zipper motif.
T, Schmidt-Dörr, P, Oertel-Buchheit, C, Pernelle, L, Bracco, M, Schnarr, M, Granger-Schnarr   +5 more
openaire   +2 more sources

Gene activation by the AraC protein can be inhibited by DNA looping between AraC and a LexA repressor that interacts with AraC: possible applications as a two‐hybrid system

Molecular Microbiology, 1998
The Escherichia coli activator and repressor proteins AraC and LexA bind DNA as homodimers. Here we show that their heterodimerization through fused cognate dimerization domains results in repression of AraC‐dependent gene activation by LexA. Repression also requires a LexA operator half‐site located several helical turns downstream of the AraC ...
M G, Kornacker, B, Remsburg, R, Menzel
openaire   +2 more sources

Independent folding of individual components in hybrid proteins

European Journal of Biochemistry, 1990
Inactivation of the Escherichia coli repressor protein, LexA, takes place through a cleavage reaction which hydrolyzes the Ala84‐Gly85 peptide bond near the center of the molecule. The mechanism of cleavage has previously been shown to be an intramolecular reaction stimulated in vitro by elevated pH or by the addition of activated RecA protein.
S N, Slilaty, M, Ouellet, M, Fung, S H, Shen   +3 more
openaire   +2 more sources

Purified lexA protein is a repressor of the recA and lexA genes

Proceedings of the National Academy of Sciences, 1981
openaire   +1 more source

Inhibition of the transcriptional repressor LexA: Withstanding drug resistance by inhibiting the bacterial mechanisms of adaptation to antimicrobials

Life Sciences, 2020
Pierangelo Bellio, Laura Cendron, Samantha Reale   +2 more
exaly  

DNA binding properties of the LexA repressor

Biochimie, 1991
M Schnarr, M Granger-Schnarr, P Oertel-Buchheit   +2 more
exaly  

Interaction of the LexA repressor and the uvrC regulatory region

FEBS Letters, 1989
R E Moses
exaly  

A model for the LexA repressor DNA complex

Proteins: Structure, Function and Bioinformatics, 1995
Rolf Boelens, Robert Kaptein, M Schnarr   +2 more
exaly  

Tetramerization of the LexA Repressor in Solution: Implications for Gene Regulation of the E.coli SOS System at Acidic pH

Journal of Molecular Biology, 2006
Debora Foguel, Jerson L Silva, Mohana-Borges R   +2 more
exaly