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PMID: 279909 Published · ppublish English Journal Article

Enzymatic breakage of the cohesive end site of phage lambda DNA: terminase (ter) reaction.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 9 ·1978-09-00 ·Pages 4199-203

Becker A, Gold M

Abstract

An in vitro system is described for measuring the endonucleolytic conversion of the phage lambda cohesive end sites in concatemeric DNA to the cohesive chromosomal ends of the mature molecule. This enzymic process, known as the ter reaction, is catalyzed by purified lambda A gene protein. The reaction is markedly stimulated by ATP, Mg2+, spermidine, and one or more uncharacterized factors present in extracts of uninfected Escherichia coli cells. In vitro, the ter reaction proceeds in the absence of proheads under conditions that are similar to those previously found necessary for the formation of a DNA-A gene protein intermediate for the initiation of packaging.

MeSH Terms
Adenosine Triphosphate/metabolism Coliphages/ultrastructure DNA, Viral/metabolism Deoxyribonucleases/metabolism Endonucleases/metabolism Magnesium/metabolism Morphogenesis Spermidine/metabolism Substrate Specificity Virus Replication
Chemicals
DNA, Viral Adenosine Triphosphate Deoxyribonucleases Endonucleases Magnesium Spermidine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Becker A
Gold M
References (32)
32 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.75.9.4199
Published
1978-09-00
Pages
4199-203
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC336079
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.9.4199 PMC Full Text View journal details
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