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PMID: 6262762 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Movement and site selection for priming by the primosome in phage phi X174 DNA replication.

Arai K, Low RL, Kornberg A

Abstract

The Escherichia coli priming system used for initiation of DNA chains on phage phi X174 single-stranded DNA is a multiprotein unit called the primosome [Arai, K. & Kornberg. A. (1981) Proc. Natl. Acad. Sci. USA 78, 69-73]. Assembled with participation of seven prepriming proteins and primase at a unique place on the phi X174 DNA template, the primosome is bound tightly to the DNA, yet moves rapidly and unidirectionally opposite to primer and DNA chain synthesis. Contributions of protein n' and dnaB protein, two components of the primosome, to movement and site selection for priming are considered in this report. Figuratively, the primosome can be likened to a locomotive that depends on protein n' as its engine and dnaB protein as the engineer. Protein n', a DNA-dependent ATPase (dATPase) appears to use the energy of hydrolysis of the nucleoside triphosphate for processive translocation of the primosome. dnaB protein, A DNA-dependent ribonucleosidetriphosphatase, depends on allosteric effects of a nucleoside triphosphate to induce changes in the structure of the single-stranded DNA at preferred sequences that enable primase to synthesize a short primer for initiation of DNA synthesis (unpublished data). These primosome properties have important implications for the progress of the replication fork of the E. coli chromosome.

MeSH Terms
Adenosine Triphosphatases/metabolism Bacterial Proteins/metabolism Bacteriophage phi X 174/metabolism DNA/metabolism DNA Primase DNA Replication DNA, Viral/biosynthesis Escherichia coli/metabolism Genes, Viral Phosphoric Monoester Hydrolases/metabolism RNA Nucleotidyltransferases/metabolism Templates, Genetic Virus Replication
Chemicals
Bacterial Proteins DNA, Viral DNA DNA Primase RNA Nucleotidyltransferases Phosphoric Monoester Hydrolases Adenosine Triphosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Arai K
Low R L
Kornberg A
References (34)
34 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
Published
1981-02-00
Pages
707-11
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC319871
Subset
IM
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