Skip to main content
bioRxiv
  • Home
  • About
  • Submit
  • ALERTS / RSS
Advanced Search
New Results

Human HELB is a processive motor protein which catalyses RPA clearance from single-stranded DNA

S Hormeno, OJ Wilkinson, C Aicart-Ramos, S Kuppa, E Antony, MS Dillingham, View ORCID ProfileF Moreno-Herrero
doi: https://doi.org/10.1101/2021.05.27.445972
S Hormeno
1Department of Macromolecular Structures, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Madrid, Spain
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
OJ Wilkinson
2DNA:Protein Interactions Unit, School of Biochemistry, University of Bristol. Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
C Aicart-Ramos
1Department of Macromolecular Structures, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Madrid, Spain
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
S Kuppa
3Department of Biochemistry and Molecular Biology, Saint Louis University, School of Medicine, St. Louis, MO 63104, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
E Antony
3Department of Biochemistry and Molecular Biology, Saint Louis University, School of Medicine, St. Louis, MO 63104, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
MS Dillingham
2DNA:Protein Interactions Unit, School of Biochemistry, University of Bristol. Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • For correspondence: mark.dillingham@bristol.ac.uk fernando.moreno@cnb.csic.es
F Moreno-Herrero
1Department of Macromolecular Structures, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Madrid, Spain
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for F Moreno-Herrero
  • For correspondence: mark.dillingham@bristol.ac.uk fernando.moreno@cnb.csic.es
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Supplementary material
  • Preview PDF
Loading

SUMMARY

Human HELB is a poorly-characterised helicase suggested to play both positive and negative regulatory roles in DNA replication and recombination. In this work, we used bulk and single molecule approaches to characterise the biochemical activities of HELB protein with a particular focus on its interactions with RPA and RPA-ssDNA filaments. HELB is a monomeric protein which binds tightly to ssDNA with a site size of ∼20 nucleotides. It couples ATP hydrolysis to translocation along ssDNA in the 5′-to-3′ direction accompanied by the formation of DNA loops and with an efficiency of 1 ATP per base. HELB also displays classical helicase activity but this is very weak in the absence of an assisting force. HELB binds specifically to human RPA which enhances its ATPase and ssDNA translocase activities but inhibits DNA unwinding. Direct observation of HELB on RPA nucleoprotein filaments shows that translocating HELB concomitantly clears RPA from single-stranded DNA.

Competing Interest Statement

The authors have declared no competing interest.

Footnotes

  • ↵4 Lead contact

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
Back to top
PreviousNext
Posted May 27, 2021.
Download PDF

Supplementary Material

Email

Thank you for your interest in spreading the word about bioRxiv.

NOTE: Your email address is requested solely to identify you as the sender of this article.

Enter multiple addresses on separate lines or separate them with commas.
Human HELB is a processive motor protein which catalyses RPA clearance from single-stranded DNA
(Your Name) has forwarded a page to you from bioRxiv
(Your Name) thought you would like to see this page from the bioRxiv website.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Human HELB is a processive motor protein which catalyses RPA clearance from single-stranded DNA
S Hormeno, OJ Wilkinson, C Aicart-Ramos, S Kuppa, E Antony, MS Dillingham, F Moreno-Herrero
bioRxiv 2021.05.27.445972; doi: https://doi.org/10.1101/2021.05.27.445972
Digg logo Reddit logo Twitter logo Facebook logo Google logo LinkedIn logo Mendeley logo
Citation Tools
Human HELB is a processive motor protein which catalyses RPA clearance from single-stranded DNA
S Hormeno, OJ Wilkinson, C Aicart-Ramos, S Kuppa, E Antony, MS Dillingham, F Moreno-Herrero
bioRxiv 2021.05.27.445972; doi: https://doi.org/10.1101/2021.05.27.445972

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Subject Area

  • Molecular Biology
Subject Areas
All Articles
  • Animal Behavior and Cognition (3686)
  • Biochemistry (7766)
  • Bioengineering (5664)
  • Bioinformatics (21228)
  • Biophysics (10551)
  • Cancer Biology (8156)
  • Cell Biology (11901)
  • Clinical Trials (138)
  • Developmental Biology (6733)
  • Ecology (10387)
  • Epidemiology (2065)
  • Evolutionary Biology (13836)
  • Genetics (9691)
  • Genomics (13051)
  • Immunology (8119)
  • Microbiology (19929)
  • Molecular Biology (7823)
  • Neuroscience (42947)
  • Paleontology (318)
  • Pathology (1276)
  • Pharmacology and Toxicology (2256)
  • Physiology (3349)
  • Plant Biology (7207)
  • Scientific Communication and Education (1309)
  • Synthetic Biology (1998)
  • Systems Biology (5527)
  • Zoology (1126)