Literature summary for 3.4.21.88 extracted from

Patterson-Fortin, L.M.; Owttrim, G.W.
A Synechocystis LexA-orthologue binds direct repeats in target genes (2008), FEBS Lett., 582, 2424-2430.

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Cloned(Commentary)

Cloned (Comment)	Organism
the amino-terminal DNA binding domain of LexA and full-length LexA ligated into pRSETB vector DNA producing pNLexA which expresses a recombinant 11.4 kDa HIS-LexA polypeptide encoding the N-terminal DNA binding domain. Expression of plasmid constructs in Escherichia coli strains DH5alpha and JM109	Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
29300	-	recombinant LexA	Synechocystis sp.

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp.	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
the amino-terminal DNA binding domain of LexA and full-length LexA	Synechocystis sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	LexA interacts with its own promoter. LexA-orthologue binds as a dimer to 12 bp direct repeats containing a CTA-N9-CTA sequence conserved in two target genes, lexA and crhR. Recombinant LexA does not bind the crhR transcript, it binds non-specifically to RNA and consequently does not appear to exert its effect on gene expression at the post-transcriptional level. Recombinant LexA binds the crhR gene as a dimer	Synechocystis sp.	?	-	?

Subunits

Subunits	Comment	Organism
More	LexA exists predominately as a monomer in solution and dimerizes upon binding to its DNA targets. The C-terminal domain is important for protein dimerization	Synechocystis sp.

Synonyms

Synonyms	Comment	Organism
LexA	-	Synechocystis sp.

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Release 2023.1 (January 2023)