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Volume 158, Issue 8

RecG binds and unwinds model DNA substrates with a preference for Holliday junctions Free

Abstract

The RecG enzyme, a superfamily 2 helicase, is present in nearly all bacteria. Here we report for the first time that the gene is also present in the genomes of most vascular plants as well as in green algae, but is not found in other eukaryotes or archaea. The precise function of RecG is poorly understood, although ample evidence shows that it plays critical roles in DNA repair, recombination and replication. We further demonstrate that RecG (RecG) DNA binding activity had a broad substrate specificity, whereas it only unwound branched-DNA substrates such as Holliday junctions (HJs), replication forks, D-loops and R-loops, with a strong preference for the HJ as a helicase substrate. In addition, RecG preferentially bound relatively long (≥40 nt) ssDNA, exhibiting a higher affinity for the homopolymeric nucleotides poly(dT), poly(dG) and poly(dC) than for poly(dA). RecG helicase activity was supported by hydrolysis of ATP or dATP in the presence of Mg, Mn, Cu or Fe. Like its orthologue, RecG is also a strictly DNA-dependent ATPase.

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2012-08-01
2024-04-20
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Mycobacterium tuberculosis RecG binds and unwinds model DNA substrates with a preference for Holliday junctions
Microbiology 158, 1982 (2012); https://doi.org/10.1099/mic.0.058693-0
/content/journal/micro/10.1099/mic.0.058693-0
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