Award details

AFM based structural/dynamic studies of a ternary replisomal complex

Reference	BB/C500579/1
Principal Investigator / Supervisor	Professor Panos Soultanas
Co-Investigators / Co-Supervisors	Professor Stephanie Allen, Professor Clive Roberts
Institution	University of Nottingham
Department	Sch of Chemistry
Funding type	Research
Value (£)	160,258
Status	Completed
Type	Research Grant
Start date	07/10/2004
End date	06/10/2007
Duration	36 months

Abstract

Elucidation of biomolecular structures by crystallography and NMR is a powerful way of understanding biological functions. However, large multi-enzyme complexes pose a difficult challenge that is amplified by the technological limitations of these techniques. Microscopy offers an alternative approach but again technological advances are needed to improve imaging in terms of resolution and environment, so that we can obtain the highest possible images in the most relevant physiological environment. Single molecular biophysical approaches, such as AFM, provide powerful opportunities towards tackling these limitations. The applicants (Dr¿s Allen and Roberts) are at the forefront of this research and have employed in situ AFM both to visualise dynamic biomolecular events involving DNA structural transitions and to study molecular interactions between a variety of protein and DNA systems. Dr Soultanas is research active in the area of protein-protein, protein-DNA and protein-ligand interactions involving DNA helicases. He is studying the interactions between replicative bacterial DNA helicase DnaB, the primase DnaG and the clamp loader protein tau. A recent collaboration between our groups has resulted in revealing the molecular architecture of the bacterial DnaB-tau complex and allowed us to build a structural model for the helicase-clamp-loader replisomal sub-assembly. We are now seeking funding to build upon this collaboration and develop the technology further in order to study the helicase-primase complex as well as the larger, more complicated helicase-primase-clamp-loader temary complex.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
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

I accept the terms and conditions of use (opens in new window)

export PDF file

back to list new search