Author
Listed:
- Derek J. Richard
(Signal Transduction Laboratory, Queensland Institute of Medical Research, Brisbane, Queensland 4029, Australia)
- Emma Bolderson
(Signal Transduction Laboratory, Queensland Institute of Medical Research, Brisbane, Queensland 4029, Australia)
- Liza Cubeddu
(Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK
School of Molecular and Microbial Biosciences, University of Sydney, Sydney, New South Wales 2006, Australia)
- Ross I. M. Wadsworth
(Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK)
- Kienan Savage
(Signal Transduction Laboratory, Queensland Institute of Medical Research, Brisbane, Queensland 4029, Australia
School of Medicine, University of Queensland)
- Girdhar G. Sharma
(Washington University School of Medicine, St Louis, Missouri 63108, USA)
- Matthew L. Nicolette
(University of Texas at Austin, Austin, Texas 78712, USA)
- Sergie Tsvetanov
(Signal Transduction Laboratory, Queensland Institute of Medical Research, Brisbane, Queensland 4029, Australia)
- Michael J. McIlwraith
(London Research Institute, Clare Hall Laboratories, Cancer Research UK, South Mimms, Hertfordshire EN6 3LD, U.K)
- Raj K. Pandita
(Washington University School of Medicine, St Louis, Missouri 63108, USA)
- Shunichi Takeda
(Kyoto University Graduate School of Medicine)
- Ronald T. Hay
(Wellcome Biocentre, University of Dundee)
- Jean Gautier
(Institute for Cancer Genetics, Columbia University Medical Center, New York, New York 10032, USA)
- Stephen C. West
(London Research Institute, Clare Hall Laboratories, Cancer Research UK, South Mimms, Hertfordshire EN6 3LD, U.K)
- Tanya T. Paull
(University of Texas at Austin, Austin, Texas 78712, USA)
- Tej K. Pandita
(Washington University School of Medicine, St Louis, Missouri 63108, USA)
- Malcolm F. White
(Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK)
- Kum Kum Khanna
(Signal Transduction Laboratory, Queensland Institute of Medical Research, Brisbane, Queensland 4029, Australia)
Abstract
DNA damage: More protection for ssDNA Single-stranded DNA (ssDNA) in a cell is highly prone to degradation, so cells shield ssDNA from nucleases by coating it with ssDNA-binding proteins (SSBs). In eukaryotes, the canonical SSB is a heterotrimer known as RPA. In this work, Khanna and colleagues characterize a second SSB from human cells, which they call hSSB1. Unlike RPA, hSSB1 is a single protein. Its primary function seems to be in the cellular response to DNA damage.
Suggested Citation
Derek J. Richard & Emma Bolderson & Liza Cubeddu & Ross I. M. Wadsworth & Kienan Savage & Girdhar G. Sharma & Matthew L. Nicolette & Sergie Tsvetanov & Michael J. McIlwraith & Raj K. Pandita & Shunich, 2008.
"Single-stranded DNA-binding protein hSSB1 is critical for genomic stability,"
Nature, Nature, vol. 453(7195), pages 677-681, May.
Handle:
RePEc:nat:nature:v:453:y:2008:i:7195:d:10.1038_nature06883
DOI: 10.1038/nature06883
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