Your browser doesn't support javascript.
loading
A newly discovered protein export machine in malaria parasites.
de Koning-Ward, Tania F; Gilson, Paul R; Boddey, Justin A; Rug, Melanie; Smith, Brian J; Papenfuss, Anthony T; Sanders, Paul R; Lundie, Rachel J; Maier, Alexander G; Cowman, Alan F; Crabb, Brendan S.
Afiliación
  • de Koning-Ward TF; The Walter & Eliza Hall Institute of Medical Research, Melbourne 3052, Australia.
Nature ; 459(7249): 945-9, 2009 Jun 18.
Article en En | MEDLINE | ID: mdl-19536257
ABSTRACT
Several hundred malaria parasite proteins are exported beyond an encasing vacuole and into the cytosol of the host erythrocyte, a process that is central to the virulence and viability of the causative Plasmodium species. The trafficking machinery responsible for this export is unknown. Here we identify in Plasmodium falciparum a translocon of exported proteins (PTEX), which is located in the vacuole membrane. The PTEX complex is ATP-powered, and comprises heat shock protein 101 (HSP101; a ClpA/B-like ATPase from the AAA+ superfamily, of a type commonly associated with protein translocons), a novel protein termed PTEX150 and a known parasite protein, exported protein 2 (EXP2). EXP2 is the potential channel, as it is the membrane-associated component of the core PTEX complex. Two other proteins, a new protein PTEX88 and thioredoxin 2 (TRX2), were also identified as PTEX components. As a common portal for numerous crucial processes, this translocon offers a new avenue for therapeutic intervention.
Asunto(s)

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Plasmodium falciparum / Proteínas Protozoarias / Malaria Falciparum / Complejos Multiproteicos Límite: Animals Idioma: En Año: 2009 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Plasmodium falciparum / Proteínas Protozoarias / Malaria Falciparum / Complejos Multiproteicos Límite: Animals Idioma: En Año: 2009 Tipo del documento: Article