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Molecular characterisation of bi-directional solute movement in ABC transporters

Reference	P08471
Principal Investigator / Supervisor	Professor Philip Poole
Co-Investigators / Co-Supervisors
Institution	University of Reading
Department	Animal and Microbial Sciences
Funding type	Research
Value (£)	164,460
Status	Completed
Type	Research Grant
Start date	01/01/1998
End date	01/01/2001
Duration	36 months

Abstract

The general amino acid permease (aap) from Rhizobium leguminosarum is the first ABC transporter of amino acids to have broad specificity for all L-amino acids. Kinetic analysis of the Aap suggests that it is an active uptake system that also influences the efflux (excretion) of amino acids. The ability to actively accumulate amino acids as well as catalyse efflux contradicts the paradigm that ABC transporters are uni-directional. If correct it also removes one of the principal differences between ABC transporters and ABC channels. The purpose of this study is to determine whether the Aap is bi-directional or whether it regulates an independent efflux system. We have identified by sequence alignment and site directed mutagenesis a region in the N-terminus of the integral membrane proteins of ABC polar amino acid transporters that governs solute specificity. Using a bank of site directed aapQ mutants reconstituted in membrane vesicles we will determine whether solute specificity is altered for both uptake and efflux.

Summary

unavailable

Committee	Closed Committee - Plant & Microbial Sciences (PMS)
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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