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R-Loop in the Replication Origin of Human Mitochondrial DNA Is Resolved by RecG, a Holliday Junction-Specific Helicase

1999; Elsevier BV; Volume: 255; Issue: 1 Linguagem: Inglês

10.1006/bbrc.1998.0133

1090-2104

Takashi Ohsato, Tsuyoshi Muta, Atsushi Fukuoh, Hideo Shinagawa, Naotaka Hamasaki, Dongchon Kang,

ATP Synthase and ATPases Research

Stable RNA-DNA hybrids (R-loops) prime the initiation of replication inEscherichia colicells. The R-loops are resolved byEscherichia coliRecG protein, a Holliday junction specific helicase. A stable RNA-DNA hybrid formation in the mitochondrial D-loop region is also implicated in priming the replication of mitochondrial DNA. Consistent with this hypothesis, the 3′ ends of the mitochondrial R-loop formed by in vitro transcription are located close to the initiation sites of the mitochondrial DNA replication. This mitochondrial R-loop is resolved by RecG in a dose-dependent manner. Since the resolution by RecG requires ATP, the resolution is dependent on the helicase activity of RecG. A linear RNA-DNA heteroduplex is not resolved by RecG, suggesting that RecG specifically recognizes the higher structure of the mitochondrial R-loop. This is the first example that R-loops of an eukaryotic origin is sensitive to a junction-specific helicase. The resolution of the mitochondrial R-loop by RecG suggests that the replication-priming R-loops have a common structural feature recognized by RecG.