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PMID: 6322184 Published · ppublish English Comparative Study 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.

RNase H confers specificity in the dnaA-dependent initiation of replication at the unique origin of the Escherichia coli chromosome in vivo and in vitro.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 81 ·No. 4 ·1984-02-00 ·Pages 1040-4

Ogawa T, Pickett GG, Kogoma T, Kornberg A

Abstract

Escherichia coli rnh mutants defective in RNase H activity display the features of previously described sdrA (stable DNA replication) and dasF (dnaA suppressor) mutants: (i) sustained DNA replication in the absence of protein synthesis, (ii) lack of requirement for dnaA protein and the origin of replication (oriC), and (iii) sensitivity of growth to a rich medium. Both the sdrA mutants (selected for continued DNA replication in the absence of protein synthesis) and the dasF mutants (selected as dnaA suppressors) are defective in RNase H activity, measured in vitro. Furthermore, a 760-base-pair fragment containing the rnh+ structural gene complements the phenotype of each of the rnh, sdrA, and dasF mutants, indicative of a single gene. One function of RNase H in vivo is in the initiation of a cycle of DNA replication at oriC dependent on dnaA+. In keeping with these results, RNase H contributes to the specificity of dnaA protein-dependent replication initiated at oriC in a partially purified enzyme system.

MeSH Terms
Bacterial Proteins/genetics Chloramphenicol/pharmacology Chromosomes, Bacterial/physiology DNA Replication Endoribonucleases/metabolism Escherichia coli/drug effects,genetics Genes Genes, Bacterial Genetic Complementation Test Genotype Mutation Phenotype Ribonuclease H Species Specificity Suppression, Genetic
Chemicals
Bacterial Proteins Chloramphenicol Endoribonucleases Ribonuclease H
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Ogawa T
Pickett G G
Kogoma T
Kornberg A
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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
DOI
10.1073/pnas.81.4.1040
Published
1984-02-00
Pages
1040-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC344759
Subset
IM
Grants
NIGMS NIH HHS · GM 07581 · United States
NIGMS NIH HHS · GM 22092 · United States
External Links
PubMed source DOI: 10.1073/pnas.81.4.1040 PMC Full Text View journal details
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