Identification and functional characterization of a poly(A)-binding protein from Leishmania infantum (LiPABP)
2011
Guerra, Natalia | Vega-Sendino, María | Pérez-Morgado, M Isabel | Ramos, Edurne | Soto, Manuel | Gonzalez, Victor M. | Martín, M Elena
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.
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