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PMID: 1256542 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

T4 gene 32 protein model for control of activity at replication fork.

Nature ·Vol. 259 ·No. 5543 ·1976-02-12 ·Pages 455-8

Moise H, Hosoda J

Abstract

Limited hydrolysis of gene 32 protein by various proteinases results in the production of three stable cleavage products. Two of these products show an affinity for native T4 DNA cellulose that the uncleaved protein does not exhibit. A model for proteolytic cleavage and for the total unwinding of DNA in advance of the replication fork is discussed in terms of this unusual binding affinity.

MeSH Terms
Binding Sites Coliphages/metabolism DNA Replication DNA, Single-Stranded/metabolism DNA, Viral/biosynthesis Models, Biological Molecular Weight Nucleic Acid Denaturation Peptide Hydrolases Protein Conformation Structure-Activity Relationship Viral Proteins/analysis,metabolism
Chemicals
DNA, Single-Stranded DNA, Viral Viral Proteins Peptide Hydrolases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Moise H
Hosoda J
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1976-02-12
Pages
455-8
Language
English
Region
England
NLM ID
0410462
Subset
IM
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