Identification and functional characterization of a poly(A)-binding protein from Leishmania infantum (LiPABP).

Natalia Guerra, María Vega-Sendino, M Isabel Pérez-Morgado, Edurne Ramos, Manuel Soto, Víctor M Gonzalez, M Elena Martín

Servicio de Bioquímica-Investigación, Hospital Ramón y Cajal, IRyCIS, Madrid, Spain.

FEBS letters 2011 Jan 3

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Gene expression regulation in Leishmania has been related to post-transcriptional events involving mainly sequences present in the 5' and 3' 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. Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Natalia Guerra, María Vega-Sendino, M Isabel Pérez-Morgado, Edurne Ramos, Manuel Soto, Víctor M Gonzalez, M Elena Martín. Identification and functional characterization of a poly(A)-binding protein from Leishmania infantum (LiPABP). FEBS letters. 2011 Jan 3;585(1):193-8