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Structural and thermodynamic characterisation of the oligomerisation and DNA interactions of the histone-like nucleoid structuring protein H-NS

Reference	C11098
Principal Investigator / Supervisor	Professor John Ladbury
Co-Investigators / Co-Supervisors	Dr Paul Driscoll
Institution	University College London
Department	Structural Molecular Biology
Funding type	Research
Value (£)	97,872
Status	Completed
Type	Research Grant
Start date	01/09/1999
End date	01/09/2001
Duration	24 months

Abstract

Although bacteria do not have nucleosomes analogous to those of eukaryotic cells, there are several abundant DNA binding proteins that appear to form chromatin-like structures and play a role in organisation of chromosomal DNA; one such protein is H-NS. Little is known about the mode of binding of this protein or its oligomeric state in the free and bound states. In this study we aim to determine the structure-function relationship for this protein in respect of its DNA binding by solving the three-dimensional solution structure and performing binding studies with a range of oligonucleotides. This will allow us a unique insight into the way in which this protein recognises DNA and how its oligomeric state is important in this process.

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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