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PMID: 7961409 Published · ppublish English Comparative Study Journal Article

Structure and transcriptional regulation of the Escherichia coli adaptive response gene aidB.

Journal of bacteriology ·Vol. 176 ·No. 21 ·1994-11-00 ·Pages 6583-9

Landini P, Hajec LI, Volkert MR

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.

Related Genes
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
References (28)
28 references, click to expand
  1. Isolation and characterization of Escherichia coli K-12 mutants unable to induce the adaptive response to simple alkylating agents.
    J Bacteriol. 1979 Sep;139(3):783-91 PMID: 383692
  2. A new pathway for DNA repair in Escherichia coli.
    Nature. 1977 May 19;267(5608):281-3 PMID: 325420
  3. Isolation of mutants of Escherichia coli with increased resistance to alkylating agents: mutants deficient in thiols and mutants constitutive for the adaptive response.
    Mol Gen Genet. 1980;180(1):85-90 PMID: 7003313
  4. Adaptation to alkylation resistance involves the induction of a DNA glycosylase.
    Nature. 1982 Apr 22;296(5859):773-5 PMID: 7040984
  5. A new gene (alkB) of Escherichia coli that controls sensitivity to methyl methane sulfonate.
    J Bacteriol. 1983 Mar;153(3):1301-7 PMID: 6337994
  6. The effects of weak acids on potassium uptake by Escherichia coli K-12 inhibition by low cytoplasmic pH.
    Biochim Biophys Acta. 1983 May 5;730(2):379-86 PMID: 6405784
  7. Structure and expression of the alkA gene of Escherichia coli involved in adaptive response to alkylating agents.
    J Biol Chem. 1984 Nov 25;259(22):13730-6 PMID: 6094528
  8. Induction and autoregulation of ada, a positively acting element regulating the response of Escherichia coli K-12 to methylating agents.
    J Bacteriol. 1985 Mar;161(3):888-95 PMID: 2982792
  9. Escherichia coli gene induction by alkylation treatment.
    Genetics. 1986 Jan;112(1):11-26 PMID: 3080354
  10. The intracellular signal for induction of resistance to alkylating agents in E. coli.
    Cell. 1986 Apr 25;45(2):315-24 PMID: 3009022
  11. Regulatory mechanisms for induction of synthesis of repair enzymes in response to alkylating agents: ada protein acts as a transcriptional regulator.
    Proc Natl Acad Sci U S A. 1986 Sep;83(17):6297-301 PMID: 3529081
  12. Molecular cloning of Mu d(bla lacZ) transcriptional and translational fusions.
    J Bacteriol. 1987 May;169(5):2026-30 PMID: 3032905
  13. The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library.
    Cell. 1987 Jul 31;50(3):495-508 PMID: 3038334
  14. Expression of the ada gene of Escherichia coli in response to alkylating agents. Identification of transcriptional regulatory elements.
    J Mol Biol. 1988 Aug 5;202(3):483-94 PMID: 3139888
  15. Altered induction of the adaptive response to alkylation damage in Escherichia coli recF mutants.
    J Bacteriol. 1989 Jan;171(1):99-103 PMID: 2536670
  16. Induction of the alkylation-inducible aidB gene of Escherichia coli by anaerobiosis.
    J Bacteriol. 1989 Feb;171(2):1196-8 PMID: 2492508
  17. Regulation of expression of the ada gene controlling the adaptive response. Interactions with the ada promoter of the Ada protein and RNA polymerase.
    J Mol Biol. 1989 Jan 20;205(2):373-85 PMID: 2648001
  18. A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress.
    J Bacteriol. 1989 Jul;171(7):3933-9 PMID: 2472381
  19. Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family.
    J Biol Chem. 1989 Sep 25;264(27):16321-31 PMID: 2777793
  20. Identification of a central regulator of stationary-phase gene expression in Escherichia coli.
    Mol Microbiol. 1991 Jan;5(1):49-59 PMID: 1849609
  21. Anaerobic induction of the alkylation-inducible Escherichia coli aidB gene involves genes of the cysteine biosynthetic pathway.
    J Bacteriol. 1992 Mar;174(6):2043-6 PMID: 1312537
  22. Acidification of Escherichia coli and Salmonella typhimurium cytoplasm reduces the mutagenic effect of N-methyl-N'-nitro-N-nitrosoguanidine.
    Mutat Res. 1993 Mar;293(3):197-204 PMID: 7679469
  23. Heterogeneity of the principal sigma factor in Escherichia coli: the rpoS gene product, sigma 38, is a second principal sigma factor of RNA polymerase in stationary-phase Escherichia coli.
    Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3511-5 PMID: 8475100
  24. Induction of the alkylation-inducible aidB gene of Escherichia coli by cytoplasmic acidification and N-ethylmaleimide.
    Mutat Res. 1994 Jan;314(1):51-6 PMID: 7504191
  25. Some chemical aspects of dose-response relationships in alkylation mutagenesis.
    Mutat Res. 1974 Jun;23(3):283-95 PMID: 4366872
  26. Electron-transferring flavoprotein of Peptostreptococcus elsdenii that functions in the reduction of acrylyl-coenzyme A.
    J Bacteriol. 1975 Dec;124(3):1447-53 PMID: 172488
  27. High-resolution 31P nuclear magnetic resonance studies of metabolism in aerobic Escherichia coli cells.
    Proc Natl Acad Sci U S A. 1977 Mar;74(3):888-91 PMID: 15257
  28. Repair of alkylated DNA in Escherichia coli. Methyl group transfer from O6-methylguanine to a protein cysteine residue.
    J Biol Chem. 1980 Nov 25;255(22):10569-71 PMID: 7000780
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1994-11-00
Pages
6583-9
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC197013
Subset
IM
Databases
GENBANK
L20915
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