ArticleNucleic acids research2011
The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 45 citations in OpenAlex.
- Processing of reversed replication forks is required for the resolution of replication-transcription conflicts.Nucleic acids research · 2026Article
- OT-Curtains: an approach for studying protein interactions with DNA ends using optical tweezers and confocal fluorescence microscopy.Nucleic acids research · 2026Article
- Processing of Reversed Replication Forks is Required for the Resolution of Replication-Transcription Conflicts.bioRxiv : the preprint server for biology · 2026Article
- Structure of an initiation complex of mycobacterial helicase-nuclease AdnAB at a blunt double-strand break reveals local melting that engages the 3' tracking strand at the ratchet pawl of the helicase motor.Nucleic acids research · 2026Article
- Insight into the biochemical mechanism of DNA helicases provided by bulk-phase and single-molecule assays.Methods (San Diego, Calif.) · 2022Review
- Human HELB is a processive motor protein that catalyzes RPA clearance from single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- RecA Is Required for the Assembly of RecN into DNA Repair Complexes on the Nucleoid.Journal of bacteriology · 2021Article
- Clutch mechanism of chemomechanical coupling in a DNA resecting motor nuclease.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Bulk and single-molecule analysis of a bacterial DNA2-like helicase-nuclease reveals a single-stranded DNA looping motor.Nucleic acids research · 2020Article
- Identification of genes required for the fitness ofMicrobial genomics · 2020Article
- Article
- Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The RecB helicase-nuclease tether mediates Chi hotspot control of RecBCD enzyme.Nucleic acids research · 2019Article
- How Does a Helicase Unwind DNA? Insights from RecBCD Helicase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2018Review
- Fluorescent single-stranded DNA-binding protein from Plasmodium falciparum as a biosensor for single-stranded DNA.PloS one · 2018Article
- Global analysis of double-strand break processing reveals in vivo properties of the helicase-nuclease complex AddAB.PLoS genetics · 2017Article
- Chi hotspots trigger a conformational change in the helicase-like domain of AddAB to activate homologous recombination.Nucleic acids research · 2016Article
- Re-evaluating the kinetics of ATP hydrolysis during initiation of DNA sliding by Type III restriction enzymes.Nucleic acids research · 2015Article
- Probing DNA helicase kinetics with temperature-controlled magnetic tweezers.Small (Weinheim an der Bergstrasse, Germany) · 2015Article
- Recombination hotspots attenuate the coupled ATPase and translocase activities of an AddAB-type helicase-nuclease.Nucleic acids research · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.