Award details

The role of protein complexes and protein localisation in regulation of bacterial nitrogen metabolism

Reference	BBS/E/J/000CA319
Principal Investigator / Supervisor	Professor Mike Merrick
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	140,363
Status	Completed
Type	Institute Project
Start date	15/10/2007
End date	14/10/2010
Duration	36 months

Abstract

Until relatively recently most bacteria were considered to be single celled organisms within which there was little, if any, cellular organisation. However in the last ten years this picture has changed radically, largely as a consequence of studies on cell division where it is now apparent that proteins have very specific locations within the cell and that these can change dramatically and rapidly. A second advance has been the recognition that many, if not most, proteins are part of multi-protein complexes which reflect the activities of functionally related proteins and may also be localised to specific positions within the cell. Furthermore these positions can change according to the environment and metabolic state of the cell. This grant will explore the ways in which interactions between proteins and the cellular localisation of proteins contribute to the way in which bacteria control fundamental metabolic processes. The work will concentrate on the area of nitrogen metabolism in the model organism Esherichia coli. We have previously shown that the flux of ammonia through the ammonia channel AmtB is controlled by the dynamic localisation of a regulatory protein, GlnK. We now plan to investigate whether multi-protein complexes are a common feature of the way in which bacteria achieve and regulate the metabolism of ammonium and other nitrogen sources. We wish to address three questions: 1. How do the intracellular pools of the effector molecules 2-oxoglutarate, ATP and ADP vary according to cellular nitrogen status and how do these impact on the regulation of ammonium uptake by AmtB? 2. How and why is a proportion of the cellular glutamine synthetase pool membrane associated? Is this localisation mediated by interaction with one or more inner membrane proteins? 3. Do the E. coli PII proteins GlnB and GlnK have more targets in the cell than are currently recognised? If so how do they regulate these targets and where are these targets located in the cell?

Summary

unavailable

Committee	Closed Committee - Plant & Microbial Sciences (PMS)
Research Topics	Microbiology
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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