Abstract
Expression of the Escherichia coli aidB gene is induced in vivo by alkylation damage in an ada-dependent pathway and by anaerobiosis or by acetate at pH 6.5 in an ada-independent fashion. In this report, we present data on aidB gene structure, function, and regulation. The aidB gene encodes a protein of ca. 60 kDa that is homologous to several mammalian acyl coenzyme A dehydrogenases. Accordingly, crude extracts from an aidB-overexpressing strain showed isovaleryl coenzyme A dehydrogenase activity. aidB overexpression also reduced N-methyl-N'-nitro-N-nitrosoguanidine-induced mutagenesis. Both ada- and acetate/pH-dependent induction of aidB are regulated at the transcriptional level, and the same transcriptional start point is used for both kinds of induction. Ada protein plays a direct role in aidB regulation: methylated Ada is able to bind to the aidB promoter region and to activate transcription from aidB in an in vitro transcription-translation system using crude E. coli extracts.
MeSH Terms
Adaptation, Physiological/genetics
Alkylation
Amino Acid Sequence
Bacterial Proteins/genetics
Base Sequence
Cloning, Molecular
DNA Damage
Escherichia coli/genetics
Escherichia coli Proteins
Fatty Acid Desaturases/genetics
Gene Expression Regulation, Bacterial
Isovaleryl-CoA Dehydrogenase
Methylnitronitrosoguanidine
Molecular Sequence Data
Mutagenesis
O(6)-Methylguanine-DNA Methyltransferase
Oxidoreductases/metabolism
Oxidoreductases Acting on CH-CH Group Donors
Promoter Regions, Genetic/genetics
Protein Binding
Recombinant Fusion Proteins
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Transcription Factors
Transcription, Genetic
Chemicals
AidB protein, E coli
Bacterial Proteins
Escherichia coli Proteins
Recombinant Fusion Proteins
Transcription Factors
Methylnitronitrosoguanidine
Oxidoreductases
Fatty Acid Desaturases
Oxidoreductases Acting on CH-CH Group Donors
Isovaleryl-CoA Dehydrogenase
Ada protein, E coli
O(6)-Methylguanine-DNA Methyltransferase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Landini P
Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655.
Hajec L I
Volkert M R
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