About the Project
see web site http://www.biosciences.bham.ac.uk/About/staff_profiles_Contact.htm?ID=31
We are interested in the biochemical properties, cellular roles, and regulation of stress response proteins in general and molecular chaperones in particular. Much of our research is on the GroEL Hsp60) chaperone protein of E. coli, and its homologues in other prokaryotes such as the nitrogen fixing bacterium Rhizobium leguminosarum, the pathogen Mycobaterium tuberculosis and its relative Mycobacterium smegmatis, and the halophilic archaeon, Haloferax volcanii. We are studying the function of these proteins using in vitro techniques and relating these to the in vivo roles of the proteins using a molecular genetic approach. Regulation of the heat shock response in different organisms is being studied by the isolation of genes for regulator proteins and, increasingly, through whole genome approaches. We are also interested in the potential applications of these proteins in aiding commercial analysis and production of heterologous proteins in E. coli. We also have a strong interest in other stress responses, particularly those that may be important for the growth and survival of enteropathogenic E. coli such as E. coli 0157. This includes in particular the response to acid. We are interested in developing models of the regulatory networks controlling the responses of different organisms to stress, and how such networks evolve over time.
___
To find out more about studying for a PhD at the University of Birmingham, including full details of the research undertaken in each school, the funding opportunities for each subject, and guidance on making your application, you can now order your copy of the new Doctoral Research Prospectus, at: www.birmingham.ac.uk/students/drp.aspx
___
Please find additional funding text below. For further funding details, please see the ‘Funding’ section.
The School of Biosciences offers a number of UK Research Council (e.g. BBSRC, NERC) PhD studentships each year. Fully funded research council studentships are normally only available to UK nationals (or EU nationals resident in the UK) but part-funded studentships may be available to EU applicants resident outside of the UK. The deadline for applications for research council studentships is 31 January each year.
Each year we also have a number of fully funded Darwin Trust Scholarships. These are provided by the Darwin Trust of Edinburgh and are for non-UK students wishing to undertake a PhD in the general area of Molecular Microbiology. The deadline for this scheme is also 31 January each year.
Funding Notes
All applicants should indicate in their applications how they intend to fund their studies. We have a thriving community of international PhD students and encourage applications at any time from students able to find their own funding or who wish to apply for their own funding (e.g. Commonwealth Scholarship, Islamic Development Bank).
The postgraduate funding database provides further information on funding opportunities available http://www.birmingham.ac.uk/postgraduate/funding/FundingFilter.aspx and further information is also available on the School of Biosciences website http://www.birmingham.ac.uk/schools/biosciences/courses/postgraduate/phd.aspx
References
some recent relevant papers:
Chatelier J, Hill F, Lund PA, Fersht A R “In vivo activities of GroEL minichaperones” Proc Natl Acad Sci USA 95 9861-9866 (1998)
Jones S, Wallington E J, George R, Lund PA “An arginine residue (arg 101) which is conserved in many GroEL homologues is required for interactions between the two heptameric rings” J Mol Biol. 282 789-800 (1988)
Erbse A, Yifrach O, Jones S and Lund PA “Chaperone activity of a chimeric GroEL protein that can exist in a single or double ring form” J Biol Chem 274 20351-20357 (1999)
Cliff MJ, Kad NM, Hay N, Lund PA, Webb MR, Burston SG, and Clarke AR “A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL” J Mol Biol 293 667-684 (1999)
Sun Z., Scott DJ, Lund PA. Isolation and Characterisation of Mutants of GroEL that are Fully Functional as Single Rings. J Mol Biol 332 715-728 (2003).
George R, Kelly SM, Price NC, Erbse A, Fisher M, Lund PA. Three GroEL homologues from Rhizobium leguminosarum have distinct in vitro properties. Biochem Biophys Res Commun. 324 822-8 (2004)
Kapatai G, Large A, Benesch JL, Robinson CV, Carrascosa JL, Valpuesta JM, Gowrinathan P, Lund PA. All three chaperonin genes in the archaeon Haloferax volcanii are individually dispensable. Mol Microbiol. 61:1583-97 (2006)
Gould P, Maguire M, Lund PA Distinct mechanisms regulate expression of the two major groEL homologues in Rhizobium leguminosarum Arch Microbiol. 2007 Jan;187:1-14 (2007)
Gould P, Burgar H, Lund PA. Homologous cpn60 genes in Rhizobium leguminosarum are not functionally equivalent. Cell Stress Chaps., in press, 2007.
Large A, Stamme C, Lange C, Duan Z, Allers T, Soppa J and Lund P. Characterization of a tightly controlled promoter of the halophilic archaeon Haloferax volcanii, and its use in the analysis of the essential cct1 gene. Molec Microbiol 2007 in press.
Recent relevant review articles and books:
Lund PA “Molecular Chaperones in the Cell” (editor), Oxford University Press (2002)
Lund PA “Molecular Chaperones” Encyclopedia of Molecular Cell Biology and Molecular Medicine, pp 487-520 ed Meyers RA pub Wiley-VCH. (2003)
Liu H and Lund PA “The role of GroES as a co-chaperone for GroEL” in “The networking of chaperones by cochaperones” Ed G Blatch. Pub: Landes Bioscience pp 75-87. (2007)
Continue with Facebook
