The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain

J Yeeles, E.J Gwynn, M.R Webb, M.S Dillingham

Research output: Contribution to journalArticle (Academic Journal)peer-review

29 Citations (Scopus)

Abstract

The oligomeric state of Superfamily I DNA helicases is the subject of considerable and ongoing debate. While models based on crystal structures imply that a single helicase core domain is sufficient for DNA unwinding activity, biochemical data from several related enzymes suggest that a higher order oligomeric species is required. In this work we characterize the helicase activity of the AddAB helicase-nuclease, which is involved in the repair of double-stranded DNA breaks in Bacillus subtilis. We show that the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3' → 5' polarity located in the AddA subunit. The AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences.
Translated title of the contributionThe AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain
Original languageEnglish
Pages (from-to)2271 - 2285
Number of pages15
JournalNucleic Acids Research
Volume39
Issue number6
DOIs
Publication statusPublished - Mar 2011

Bibliographical note

Other: First published on line November 10th 2010

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