Identification and functional characterization of a poly(A)-binding protein from <i>Leishmania infantum</i> (<i>Li</i>PABP)

  1. Guerra, Natalia 1
  2. Vega-Sendino, María 2
  3. Pérez-Morgado, M. Isabel 1
  4. Ramos, Edurne 1
  5. Soto, Manuel 2
  6. Gonzalez, Víctor M. 1
  7. Martín, M. Elena 1
  1. 1 Servicio de Bioquímica-Investigación, Hospital Ramón y Cajal, IRyCIS, 28034 Madrid, Spain
  2. 2 Centro de Biología Molecular Severo Ochoa, Departamento de Biología Molecular, Universidad Autónoma de Madrid, CSIC-UAM, 28049 Madrid, Spain
Revista:
FEBS Letters

ISSN: 0014-5793

Año de publicación: 2010

Volumen: 585

Número: 1

Páginas: 193-198

Tipo: Artículo

DOI: 10.1016/J.FEBSLET.2010.11.042 GOOGLE SCHOLAR lock_openAcceso abierto editor

Otras publicaciones en: FEBS Letters

Resumen

Gene expression regulation in Leishmania has been related to post-transcriptional events involving mainly sequences present in the 50 and 30 untranslated regions. PABPs are high-affinity poly(A)-binding proteins that are implicated in the regulation of translation initiation, RNA stability and other important biological processes. We describe a PABP from Leishmania infantum (LiPABP) that shows a very high homology with PABPs from other eukaryotic organisms, including mammals and other parasites. LiPABP conserves the main domains present in other PABPs, maintains poly(A)-binding properties and is phosphorylated by p38 mitogen-activated protein kinase. Using the sera from dogs infected with L. infantum, we demonstrate that LiPABP is expressed in L. infantum promastigotes.

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Información de financiación

Financiadores

  • Fondo de Investigaciones Sanitarias (FIS) of the Ministerio de Ciencia e Innovación
    • PI05/0453
    • PI08/0101

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