Identification and functional characterization of a poly(A)-binding protein from Leishmania infantum (LiPABP)
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...
| Autores: | , , , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2010 |
| País: | España |
| Institución: | Universidad Complutense de Madrid (UCM) |
| Repositorio: | Docta Complutense |
| Idioma: | inglés |
| OAI Identifier: | oai:docta.ucm.es:20.500.14352/97966 |
| Acceso en línea: | https://hdl.handle.net/20.500.14352/97966 |
| Access Level: | acceso abierto |
| Palabra clave: | Poly(A)-binding protein Translation regulation Leishmania infantum Biología 24 Ciencias de la Vida |
| Sumario: | 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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