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Identification and functional characterization of a poly(A)‐binding protein from Leishmania infantum ( Li PABP)
Author(s) -
Guerra Natalia,
Vega-Sendino María,
Pérez-Morgado M. Isabel,
Ramos Edurne,
Soto Manuel,
Gonzalez Víctor M.,
Martín M. Elena
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.11.042
Subject(s) - leishmania infantum , leishmania , poly(a) binding protein , untranslated region , biology , gene , microbiology and biotechnology , messenger rna , rna binding protein , biochemistry , genetics , leishmaniasis , visceral leishmaniasis , parasite hosting , world wide web , computer science
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 ( Li PABP) that shows a very high homology with PABPs from other eukaryotic organisms, including mammals and other parasites. Li PABP 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 Li PABP is expressed in L. infantum promastigotes.