%0 Journal Article
%A Guerra Pérez, Natalia
%A Vega-Sendino, María
%A Pérez-Morgado, Isabel
%A Ramos, Edurne
%A Soto, Manuel
%A Gonzalez, Victor
%A Martín, Elena
%T Identification and functional characterization of a poly(A)-binding protein from Leishmania infantum (LiPABP)
%D 2010
%@ 0014-5793
%U https://hdl.handle.net/20.500.14352/97966
%X 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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