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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

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 form...

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Bibliographic Details
Published in:FEMS microbiology letters 2004-09, Vol.238 (1), p.255-262
Main Authors: Lightbody, Kirsty L., Renshaw, Philip S., Collins, Michelle L., Wright, Rebecca L., Hunt, Debbie M., Gordon, Stephen V., Hewinson, R. Glyn, Buxton, Roger S., Williamson, Richard A., Carr, Mark D.
Format: Article
Language:English
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Summary: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.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.2004.tb09764.x