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Structure and function of Sso10; a novel architectural DNA binding protein
Reference
C16461
Principal Investigator / Supervisor
Prof. Malcolm White
Co-Investigators /
Co-Supervisors
Professor Garry Taylor
Institution
University of St Andrews
Department
Biology
Funding type
Research
Value (£)
172,828
Status
Completed
Type
Research Grant
Start date
01/06/2002
End date
31/05/2005
Duration
36 months
Abstract
We have identified a new architectural double-stranded DNA binding protein, Sso10, conserved in all archaea and some eukaryotes. Sso10 is a highly abundant, dimeric protein of 10 kDa subunits that binds dsDNA with high affinity and no detectable sequence specificity. We predict that Sso10 is a major component of archaeal chromatin, with possible roles in DNA compaction and organisation. We have solved the structure of the protein and propose a model for its interaction with dsDNA. We will address the role of Sso10 by analysing its interaction with DNA and other proteins, identifying important residues and post-translational modifications, and examining the influence of the protein on DNA replication, repair and recombination.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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