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

Kirsty L. Lightbody; Philip S. Renshaw; Michelle L. Collins; Rebecca L. Wright; Debbie M. Hunt; Stephen V. Gordon; R. Glyn Hewinson; Roger S. Buxton; Richard A. Williamson; Mark D. Carr

doi:10.1111/j.1574-6968.2004.tb09764.x

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

Kirsty L. Lightbody
, Philip S. Renshaw
, Michelle L. Collins
, Rebecca L. Wright
, Debbie M. Hunt
, Stephen V. Gordon
, R. Glyn Hewinson
, Roger S. Buxton
, Richard A. Williamson
, Mark D. Carr

Bovine TB, diseases and control

Research output: Contribution to journal › Article › peer-review

44 Citations (Scopus)

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.

Original language	English
Pages (from-to)	255-262
Number of pages	8
Journal	FEMS Microbiology Letters
Volume	238
Issue number	1
Early online date	29 Jul 2004
DOIs	https://doi.org/10.1111/j.1574-6968.2004.tb09764.x
Publication status	Published - 01 Sept 2004

Keywords

CFP-10
ESAT-6
ESAT-6 family members
Protein-protein interaction
Tuberculosis

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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Lightbody, K. L., Renshaw, P. S., Collins, M. L., Wright, R. L., Hunt, D. M., Gordon, S. V., Hewinson, R. G., Buxton, R. S., Williamson, R. A., & 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 Microbiology Letters, 238(1), 255-262. https://doi.org/10.1111/j.1574-6968.2004.tb09764.x

Lightbody, Kirsty L. ; Renshaw, Philip S. ; Collins, Michelle L. et al. / 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. In: FEMS Microbiology Letters. 2004 ; Vol. 238, No. 1. pp. 255-262.

@article{e183a2592ecc47f984ada60ddbdebe01,

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",

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.",

keywords = "CFP-10, ESAT-6, ESAT-6 family members, Protein-protein interaction, Tuberculosis",

author = "Lightbody, \{Kirsty L.\} and Renshaw, \{Philip S.\} and Collins, \{Michelle L.\} and Wright, \{Rebecca L.\} and Hunt, \{Debbie M.\} and Gordon, \{Stephen V.\} and Hewinson, \{R. Glyn\} and Buxton, \{Roger S.\} and Williamson, \{Richard A.\} and Carr, \{Mark D.\}",

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Lightbody, KL, Renshaw, PS, Collins, ML, Wright, RL, Hunt, DM, Gordon, SV, Hewinson, RG, Buxton, RS, Williamson, RA & Carr, MD 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 Microbiology Letters, vol. 238, no. 1, pp. 255-262. https://doi.org/10.1111/j.1574-6968.2004.tb09764.x

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, Kirsty L.; Renshaw, Philip S.; Collins, Michelle L. et al.
In: FEMS Microbiology Letters, Vol. 238, No. 1, 01.09.2004, p. 255-262.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Characterisation of complex formation between members of the Mycobacterium tuberculosis complex CFP-10/ESAT-6 protein family

T2 - Towards an understanding of the rules governing complex formation and thereby functional flexibility

AU - Lightbody, Kirsty L.

AU - Renshaw, Philip S.

AU - Collins, Michelle L.

AU - Wright, Rebecca L.

AU - Hunt, Debbie M.

AU - Gordon, Stephen V.

AU - Hewinson, R. Glyn

AU - Buxton, Roger S.

AU - Williamson, Richard A.

AU - Carr, Mark D.

PY - 2004/9/1

Y1 - 2004/9/1

N2 - 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.

AB - 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.

KW - CFP-10

KW - ESAT-6

KW - ESAT-6 family members

KW - Protein-protein interaction

KW - Tuberculosis

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DO - 10.1111/j.1574-6968.2004.tb09764.x

M3 - Article

C2 - 15336430

AN - SCOPUS:4444243999

SN - 0378-1097

VL - 238

SP - 255

EP - 262

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 1

ER -

Lightbody KL, Renshaw PS, Collins ML, Wright RL, Hunt DM, Gordon SV et al. 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 Microbiology Letters. 2004 Sept 1;238(1):255-262. Epub 2004 Jul 29. doi: 10.1111/j.1574-6968.2004.tb09764.x

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

Keywords

UN SDGs

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