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Regulation of UvrD Helicase Activity by MutL.

Abstract：

:Escherichia coli UvrD is a superfamily 1 helicase/translocase involved in multiple DNA metabolic processes including methyl-directed mismatch DNA repair. Although a UvrD monomer can translocate along single-stranded DNA, a UvrD dimer is needed for processive helicase activity in vitro. E. coli MutL, a regulatory protein involved in methyl-directed mismatch repair, stimulates UvrD helicase activity; however, the mechanism is not well understood. Using single-molecule fluorescence and ensemble approaches, we find that a single MutL dimer can activate latent UvrD monomer helicase activity. However, we also find that MutL stimulates UvrD dimer helicase activity. We further find that MutL enhances the DNA-unwinding processivity of UvrD. Hence, MutL acts as a processivity factor by binding to and presumably moving along with UvrD to facilitate DNA unwinding.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Ordabayev YA,Nguyen B,Niedziela-Majka A,Lohman TM

doi

10.1016/j.jmb.2018.08.022

subject

Has Abstract

pub_date

2018-10-19 00:00:00

pages

4260-4274

issue

21

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(18)30591-6

journal_volume

430

pub_type

杂志文章

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