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PMID: 2509902 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The LexA protein does not bind specifically to the two SOS box-like sequences immediately 5' to the phr gene.

Mutation research ·Vol. 218 ·No. 3 ·1989-11-00 ·Pages 207-10

Payne NS, Sancar A

Abstract

There are two SOS box-like sequences located at the regions -161 to -142 and -69 to -50 with regard to the initiation codon of phr. Ihara et al. (1987) constructed a phr'-'lacZ fusion plasmid in which these sequences and the amino terminal end of the phr gene was fused to lacZ and therefore lacZ was under the regulatory control of phr promoter-operator. The authors found that in cells carrying this plasmid beta-galactosidase was inducible by UV and UV-mimetic agents and concluded that phr was controlled by the LexA repressor. We wished to confirm these results by theoretical analysis of the SOS-like sequences by the method developed by Berg (1987) as well as by measuring the binding of LexA protein to the putative SOS boxes by a novel gel retardation assay. Both theoretical analysis and experimental results indicate that the putative SOS boxes immediately 5' to phr have no specific affinity for LexA protein.

MeSH Terms
Bacterial Proteins/metabolism Base Sequence Binding Sites Cloning, Molecular DNA Repair DNA, Bacterial/metabolism Deoxyribodipyrimidine Photo-Lyase/genetics Escherichia coli/genetics Genes, Bacterial/drug effects,radiation effects Lac Operon Lyases/genetics Repressor Proteins/metabolism SOS Response, Genetics Serine Endopeptidases Transcription Factors/metabolism Ultraviolet Rays beta-Galactosidase/genetics
Chemicals
Bacterial Proteins DNA, Bacterial LexA protein, Bacteria Repressor Proteins Transcription Factors beta-Galactosidase Serine Endopeptidases Lyases Deoxyribodipyrimidine Photo-Lyase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Payne N S
University of North Carolina, School of Medicine, Department of Biochemistry, Chapel Hill 27599.
Sancar A
Article Info
Journal
Mutation research
Abbr.
Mutat Res
ISSN
0027-5107
Published
1989-11-00
Pages
207-10
Language
English
Region
Netherlands
NLM ID
0400763
Subset
IM
Grants
NIGMS NIH HHS · GM31082 · United States
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