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Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo
Author(s) -
Wooff Esen,
Michell Stephen Ll.,
Gordon Stephen V.,
Chambers Mark A.,
Bardarov Stoyan,
Jacobs William R.,
Hewinson R. Glyn,
Wheeler Paul R.
Publication year - 2002
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2002.02771.x
Subject(s) - auxotrophy , biology , complementation , mutant , mycobacterium tuberculosis , genetics , transposon mutagenesis , virulence , biochemistry , gene , transposable element , microbiology and biotechnology , tuberculosis , medicine , pathology
Summary Sulphur is essential for some of the most vital biological activities such as translation initiation and redox maintenance, and genes involved in sulphur metabolism have been implicated in virulence. Mycobacterium tuberculosis has three predicted genes for the prototrophic acquisition of sulphur as sulphate: cysA , part of an ABC transporter, and cysA2 and A3 , SseC sulphotransferases. Screening for amino acid auxotrophs of Mycobacterium bovis BCG, obtained by transposon mutagenesis, was used to select methionine auxotrophs requiring a sulphur‐containing amino acid for growth. We have characterized one of these auxotrophs as being disrupted in cysA . Both the cysA mutant and a previously identified mutant in an upstream gene, subI , were functionally characterized as being completely unable to take up sulphate. Complementation of the cysA mutant with the wild‐type gene from M. tuberculosis restored prototrophy and the ability to take up sulphate with the functional characteristics of an ABC transporter. Hence, it appears that this is the sole locus encoding inorganic sulphur transport in the M. tuberculosis complex