Journal of Molecular Biology
Volume 201, Issue 2, 20 May 1988, Pages 261-271
Functional sites of the Ada regulatory protein of Escherichia coli: Analysis by amino acid substitutions☆
References (35)
- et al.
Methods Enzymol.
(1983) - et al.
Gene
(1982) - et al.
J. Biol. Chem.
(1982) - et al.
Mutat. Res.
(1987) - et al.
J. Biol. Chem.
(1984) - et al.
J. Biol. Chem.
(1985) - et al.
Mutat. Res.
(1985) - et al.
Trends Genet.
(1987) Methods Enzymol.
(1975)Mutat. Res.
(1987)
Gene
(1982)
Carcinogenesis
(1986)
Biochemistry
(1981)
J. Bacteriol.
(1978)
Nucl. Acids Res.
(1986)
Nature (London)
(1982)
Cited by (48)
Inducible repair of alkylated DNA in microorganisms
2015, Mutation Research - Reviews in Mutation ResearchCitation Excerpt :Because both catalytic cysteine residue substitutions generally diminish Ada activation capacity, it can be concluded that the mechanism accepting methyl moieties induces the conformational changes, which enhance transcription factor activity. The C69H mutant retained only slight induction potential and otherwise the C321A mutant transformed into a constitutive activator [81,87,88]. The main role for C-Ada19 is to provide the site for Ada interaction with RNAP.
Induction of SOS response, cellular efflux and oxidative stress response genes by chlorambucil in DNA repair-deficient Escherichia coli cells (ada, ogt and mutS)
2003, Mutation Research - Fundamental and Molecular Mechanisms of MutagenesisChlorambucil-induced high mutation rate and suicidal gene downregulation in a base excision repair-deficient Escherichia coli strain
2002, Mutation Research - Fundamental and Molecular Mechanisms of MutagenesisThe role of DNA repair in the prevention of cancer
1996, Molecular Aspects of MedicineInduction of the adaptive response of Escherichia coli to alkylation damage by the environmental mutagen, methyl chloride
1993, Mutation Research-DNA Repair
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This work has been supported by grants from the Ministry of Education, Science and Culture (61065007) and from the Institute of Protein Engineering.
Copyright © 1988 Published by Elsevier Ltd.