Structure and transcriptional regulation of the Escherichia coli adaptive response gene aidB
Department of Molecular Genetics and Microbiology
Adaptation, Physiological; Alkylation; Amino Acid Sequence; Bacterial Proteins; Base Sequence; Cloning, Molecular; DNA Damage; Escherichia coli; *Escherichia coli Proteins; Fatty Acid Desaturases; *Gene Expression Regulation, Bacterial; Isovaleryl-CoA Dehydrogenase; Methylnitronitrosoguanidine; Molecular Sequence Data; Mutagenesis; O(6)-Methylguanine-DNA Methyltransferase; Oxidoreductases; *Oxidoreductases Acting on CH-CH Group Donors; Promoter Regions (Genetics); Protein Binding; Recombinant Fusion Proteins; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Transcription Factors; *Transcription, Genetic
Life Sciences | Medicine and Health Sciences
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.
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Citation: J Bacteriol. 1994 Nov;176(21):6583-9.
Journal of bacteriology
Landini, Paolo; Hajec, Laurel I.; and Volkert, Michael R., "Structure and transcriptional regulation of the Escherichia coli adaptive response gene aidB" (1994). Open Access Articles. 662.