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Literature summary for 3.4.21.88 extracted from

  • Giese, K.C.; Michalowski, C.B.; Little, J.W.
    RecA-dependent cleavage of LexA dimers (2008), J. Mol. Biol., 377, 148-161.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli as wild type, mutants and as truncated proteins Escherichia coli

Protein Variants

Protein Variants Comment Organism
K156A site directed mutagenesis Escherichia coli
additional information K156A, L89P, Q92W, E152A quadruple mutant, K156A, Q92W, E152A mutant variant -89, K156A, L89P, E152A mutant variant -92, K156A, L89P, Q92W mutant variant -152, K156A, Q92W mutant variant, Q92W S119A mutant variant, expression of truncated variants Escherichia coli
S119A site directed mutagenesis Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
RecA DNA repair -inducing treatments activate RecA, which inactivates LexA by a specific cleavage reaction, leading to derepression of the SOS regulon, RecA stimulates the transition of LexA from its noncleavable to its cleavable conformation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
no activity in Streptococcus thermophilus
-
a small DNA region upstream of the recA transcriptional start site carries all the information needed for normal regulation of the S. thermophilus recA gene
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information crosslinked with glutaraldehyde Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
of the recombinant protein und its truncated variants by Ni–nitrilotriacetic acid column chromatography Escherichia coli

Subunits

Subunits Comment Organism
dimer under physiological conditions, is cleaved by RecA, dimmers dissociate slowly Escherichia coli

Synonyms

Synonyms Comment Organism
LexA
-
Escherichia coli
LexA
-
no activity in Streptococcus thermophilus
LexA repressor
-
Escherichia coli