Characterisation of complex formation between members of the Mycobacterium tuberculosis complex CFP-10/ESAT-6 protein family: towards an understanding of the rules governing complex formation and thereby functional flexibility

Lightbody, K.L. and Renshaw, P.S. and Collins, M.L. and Wright, R.L. and Hunt, D.M. and Gordon, S.V. and Hewinson, R.G. and Buxton, R.S. and Williamson, R.A. and Carr, M.D. (2004) Characterisation of complex formation between members of the Mycobacterium tuberculosis complex CFP-10/ESAT-6 protein family: towards an understanding of the rules governing complex formation and thereby functional flexibility. FEMS Microbiol Lett, 238 (1). pp. 255-262. ISSN 0378-1097. (The full text of this publication is not available from this repository)

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Abstract

We have previously shown that the secreted M. tuberculosis complex proteins CFP-10 and ESAT-6 form a tight, 1:1 complex, which may represent their functional form. In the work reported here a combination of yeast two-hybrid and biochemical analysis has been used to characterise complex formation between two other pairs of CFP-10/ESAT-6 family proteins (Rv0287/Rv0288 and Rv3019c/Rv3020c) and to determine whether complexes can be formed between non-genome paired members of the family. The results clearly demonstrate that Rv0287/Rv0288 and Rv3019c/3020c form tight complexes, as initially observed for CFP-10/ESAT-6. The closely related Rv0287/Rv0288 and Rv3019c/Rv3020c proteins are also able to form non-genome paired complexes (Rv0287/Rv3019c and Rv0288/Rv3020c), but are not capable of binding to the more distantly related CFP-10/ESAT-6 proteins.

Item Type: Article
Additional information: 0378-1097 (Print) Journal Article Research Support, Non-U.S. Gov't
Uncontrolled keywords: Antigens, Bacterial/genetics/*metabolism Bacterial Proteins/genetics/*metabolism Genome, Bacterial *Multiprotein Complexes Mycobacterium tuberculosis/*metabolism Phylogeny Protein Binding Sequence Homology Two-Hybrid System Techniques beta-Galactosidase/analysis
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Richard Williamson
Date Deposited: 09 Sep 2008 15:04
Last Modified: 14 Jan 2010 14:20
Resource URI: http://kar.kent.ac.uk/id/eprint/5310 (The current URI for this page, for reference purposes)
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