Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/14384
Title: 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.
Authors: Lightbody, KL
Renshaw, PS
Collins, ML
Wright, RL
Hunt, DM
Gordon, SV
Hewinson, RG
Buxton, RS
Williamson, RA
Carr, MD
First Published: 1-Sep-2004
Citation: FEMS MICROBIOL LETT, 2004, 238 (1), pp. 255-262
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.
DOI Link: 10.1016/j.femsle.2004.07.043
ISSN: 0378-1097
Links: http://hdl.handle.net/2381/14384
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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