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PMID: 4522804 Published · ppublish English Journal Article

Photochemical attachment of lac repressor to bromodeoxyuridine-substituted lac operator by ultraviolet radiation.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 71 ·No. 3 ·1974-03-00 ·Pages 947-51

Lin SY, Riggs AD

Abstract

The transducing phage lambdah80dlac carries the lac operator, whereas wild-type lambdah80 does not. We find that in high salt (0.18 M KCl), ultraviolet radiation causes the formation of a very stable complex between repressor and 5-bromodeoxyuridine (BrdU)-substituted lambdah80dlac but not to BrdU-lambdah80 DNA. Studies with inducers of the lac operon confirm the specificity of attachment. In low slat (0.01 M KCl), ultraviolet radiation will also attach repressor nonspecifically to BrdU-lambdah80 DNA. The stability of the complex suggests that covalent bonds are formed. We also report that another regulatory protein, the catabolite gene activator protein, can be attached similarly to DNA.

MeSH Terms
Binding Sites Bromodeoxyuridine/metabolism Coliphages/metabolism DNA, Viral/biosynthesis,metabolism Genes, Regulator/radiation effects Lactose/metabolism Lysogeny Operon/radiation effects Osmolar Concentration Phosphorus Radioisotopes Photochemistry Potassium Chloride Protein Binding/radiation effects Radiation Effects Transduction, Genetic Ultraviolet Rays Viral Proteins/metabolism
Chemicals
DNA, Viral Phosphorus Radioisotopes Viral Proteins Potassium Chloride Bromodeoxyuridine Lactose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lin S Y
Riggs A D
References (25)
25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.71.3.947
Published
1974-03-00
Pages
947-51
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC388134
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.71.3.947 PMC Full Text View journal details
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