Mycobacterium tuberculosis transporter MmpL7 is a potential substrate for kinase PknD.
Biochem Biophys Res Commun
; 348(1): 6-12, 2006 Sep 15.
Article
em En
| MEDLINE
| ID: mdl-16879801
The Mycobacterium tuberculosis serine/threonine protein kinases are attractive potential drug targets, and protein kinase D (PknD) is particularly interesting, as it is autophosphorylated on 11 residues, binds proteins containing forkhead associated domains, and contains a beta-propeller motif that likely functions as an anchoring sensor domain. We created a pknD knockout of a clinical M. tuberculosis isolate, and found that on in vitro phosphorylation of cell wall fractions it lacked a family of phosphorylated polypeptides seen in the WT. Mass spectrometry identified the phosphorylated polypeptides as MmpL7, a transporter of the RND family. MmpL7 is essential for virulence, presumably because it transports polyketide virulence factors such as phthiocerol dimycocerosate (PDIM) to the cell wall. Phosphorylation of the MmpL family of transporters has not been previously described, but these results suggest that PknD, and perhaps other serine/threonine kinases, could regulate their critical role in the formation of the M. tuberculosis envelope.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Membrana Transportadoras
/
Proteínas Quinases
/
Proteínas de Bactérias
/
Mycobacterium tuberculosis
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Venezuela
País de publicação:
Estados Unidos