PMID:9009281
| Citation |
Fukuoh, A, Iwasaki, H, Ishioka, K and Shinagawa, H (1997) ATP-dependent resolution of R-loops at the ColE1 replication origin by Escherichia coli RecG protein, a Holliday junction-specific helicase. EMBO J. 16:203-9 |
|---|---|
| Abstract |
The RecG protein of Escherichia coli is a DNA helicase that promotes branch migration of the Holliday junctions. We found that overproduction of RecG protein drastically decreased copy numbers of ColE1-type plasmids, which require R-loop formation between the template DNA and a primer RNA transcript (RNA II) for the initiation of replication. RecG efficiently inhibited in vitro ColE1 DNA synthesis in a reconstituted system containing RNA polymerase, RNase HI and DNA polymerase I. RecG promoted dissociation of RNA II from the R-loop in a manner that required ATP hydrolysis. These results suggest that overproduced RecG inhibits the initiation of replication by prematurely resolving the R-loops formed at the replication origin region of these plasmids with its unique helicase activity. The possibility that RecG regulates the initiation of a unique mode of DNA replication, oriC-independent constitutive stable DNA replication, by its activity in resolving R-loops is discussed. |
| Links |
PubMed PMC1169627 Online version:10.1093/emboj/16.1.203 |
| Keywords |
Adenosine Triphosphate/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/physiology; Bacteriocin Plasmids/genetics; DNA Helicases/genetics; DNA Helicases/physiology; DNA Replication/physiology; DNA, Bacterial/biosynthesis; DNA, Bacterial/chemistry; DNA, Bacterial/metabolism; Escherichia coli/genetics; Escherichia coli Proteins; Gene Dosage; Hydrolysis; Nucleic Acid Conformation; RNA, Bacterial/metabolism; Replication Origin |
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