RT Journal Article
T1 Identification and functional characterization of a poly(A)-binding protein from Leishmania infantum (LiPABP)
A1 Guerra Pérez, Natalia
A1 Vega-Sendino, María
A1 Pérez-Morgado, Isabel
A1 Ramos, Edurne
A1 Soto, Manuel
A1 Gonzalez, Victor
A1 Martín, Elena
A2 Ibba, Michael
AB 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.
PB Federation of European Biochemical Societies
SN 0014-5793
YR 2010
FD 2010
LK https://hdl.handle.net/20.500.14352/97966
UL https://hdl.handle.net/20.500.14352/97966
LA eng
NO 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
NO Comunidad de Madrid
DS Docta Complutense
RD 15 abr 2025