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oai:docta.ucm.es:20.500.14352/979662024-09-06T23:58:53Zcom_20.500.14352_14col_20.500.14352_15

Guerra Pérez, Natalia Vega-Sendino, María Pérez-Morgado, Isabel Ramos, Edurne Soto, Manuel Gonzalez, Victor Martín, Elena 2024-02-01T18:27:34Z 2024-02-01T18:27:34Z 2010 Guerra Natalia, Vega-Sendino María, Pérez-Morgado M. Isabel, Ramos Edurne, Soto Manuel, Gonzalez Víctor M. and Martín M. Elena (2011), Identification and functional characterization of a poly(A)-binding protein from Leishmania infantum (LiPABP), FEBS Letters, 585, doi: 10.1016/j.febslet.2010.11.042 0014-5793 10.1016/j.febslet.2010.11.042 https://hdl.handle.net/20.500.14352/97966 1873-3468 https://doi.org/10.1016/j.febslet.2010.11.042 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. eng open access Identification and functional characterization of a poly(A)-binding protein from Leishmania infantum (LiPABP) journal article