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PMID: 5725 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Bacteriophage T5-induced endonucleases that introduce site-specific single-chain interruptions in duplex DNA.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 73 ·No. 5 ·1976-05-00 ·Pages 1576-80

Rogers SG, Rhoades M

Abstract

Four site-specific endodeoxyribonucleases have been partially purified from extracts of bacteriophage T5-infected Escherichia coli by gel filtration and affinity chromatography on single- and double-stranded DNA. The enzymes were detected and characterized by agarose gel electrophoresis of alkali-denatured digestion products. None of the four is found in uninfected cells. In the presence of a divalent cation, all four endonucleases make ligase-repairable, single-chain interruptions at specific sites in the duplex DNA of several bacteriophages (lambda, T7, and T5) and a mammalian virus (adenovirus 2). These activities are not stimulated by ATP. None of the four is active on single-stranded DNA. The fragments produced by each enzyme from ligase-repaired T5 DNA do not correspond to those derived from mature T5 DNA. Each of the enzymes is able to cleave the intact strand of T5 DNA.

MeSH Terms

Coliphages/enzymology DNA, Viral/metabolism Endonucleases/metabolism Hydrogen-Ion Concentration Kinetics Nucleic Acid Denaturation Polynucleotide Ligases/metabolism Structure-Activity Relationship

Chemicals

DNA, Viral Endonucleases Polynucleotide Ligases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Rogers S G

Rhoades M

References (27)

27 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.73.5.1576

Published

1976-05-00

Pages

1576-80

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC430341

Subset

External Links

PubMed source DOI: 10.1073/pnas.73.5.1576 PMC Full Text View journal details

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