Expression of the human RNA-binding protein HuR in Trypanosoma brucei increases the abundance of mRNAs containing AU-rich regulatory elements

The salivarian trypanosome Trypanosoma brucei infects mammals and is transmitted by tsetse flies. The mammalian 'bloodstream form' trypanosome has a variant surface glycoprotein coat and relies on glycolysis while the procyclic form from tsetse flies has EP protein on the surface and has a...

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Detalles Bibliográficos
Autor principal: Quijada, L.
Otros Autores: Guerra-Giraldez, C., Drozdz, M., Hartmann, C., Irmer, H., Ben-Dov, C., Cristodero, M., Ding, M., Clayton, C.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2002
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
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024 7 |2 scopus  |a 2-s2.0-0037109118 
024 7 |2 cas  |a 3' Untranslated Regions; Adenine, 73-24-5; Antigens, Surface; ELAV-like protein 1; Phosphoglycerate Kinase, EC 2.7.2.3; Protozoan Proteins; RNA, Messenger; RNA, Protozoan; RNA-Binding Proteins; Uracil, 66-22-8 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a NARHA 
100 1 |a Quijada, L. 
245 1 0 |a Expression of the human RNA-binding protein HuR in Trypanosoma brucei increases the abundance of mRNAs containing AU-rich regulatory elements 
260 |c 2002 
270 1 0 |m Clayton, C.; ZMBH, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany; email: cclayton@zmbh.uni-heidelberg.de 
506 |2 openaire  |e Política editorial 
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520 3 |a The salivarian trypanosome Trypanosoma brucei infects mammals and is transmitted by tsetse flies. The mammalian 'bloodstream form' trypanosome has a variant surface glycoprotein coat and relies on glycolysis while the procyclic form from tsetse flies has EP protein on the surface and has a more developed mitochondrion. We show here that the mRNA for the procyclic-specific cytosolic phosphoglycerate kinase PGKB, like that for EP proteins, contains a regulatory AU-rich element (ARE) that destabilises the mRNA in bloodstream forms. The human HuR protein binds to, and stabilises, mammalian mRNAs containing AREs. Expression of HuR in bloodstream-form trypanosomes resulted in growth arrest and in stabilisation of the EP, PGKB and pyruvate, phosphate dikinase mRNAs, while three bloodstream-specific mRNAs were reduced in abundance. The synthesis and abundance of unregulated mRNAs and proteins were unaffected. Our results suggest that regulation of mRNA stability by AREs arose early in eukaryotic evolution.  |l eng 
536 |a Detalles de la financiación: EMBO 
536 |a Detalles de la financiación: Deutsche Forschungsgemeinschaft 
536 |a Detalles de la financiación: We thank Henry Furneaux (Memorial Sloan Kettering Cancer Center, New York, NY) for HuR and c-fos plasmids, and for the anti-HuR monoclonal antibody. We thank Steve Beverley (University of Washington, MO, USA) and Keith Matthews (Manchester University, UK) for very useful criticism and suggestions, Shula Michaeli (Bar-Ilan University, Israel) for the SRP RNA clone and Paul Michels (ICP, Brussels) for anti-PGK. We thank other members of the laboratory, particularly A. Estévez, for discussions, and L. Krauth-Siegel, BZH, Heidelberg, for the DHLADH antibody. We thank Gitta Erdmann for contributions made during an undergraduate laboratory rotation. L.Q. was supported by an EMBO fellowship, and C.G. by a DAAD scholarship. C.B.-D. contributed during a short-term visit funded by the DAAD. The rest of the support came from the Deutsche Forschungsgemeinschaft. 
593 |a ZMBH, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany 
593 |a Centro de Biología Molecular 'SO', Lab. CX-203, Universidad Autónoma de Madrid, Cantoblanco, E-28049 Madrid, Spain 
593 |a Friedrich Miescher Institute for Biomedical Research, PO Box 2543, 4002 Basel, Switzerland 
593 |a Yale University School of Medicine, LLCI 8o1, 333 Cedar Street, New Haven, CT 06520-8022, United States 
593 |a INGEBI, Vuelta de Obligado 2490, (1428) Buenos Aires, Argentina 
690 1 0 |a ADENINE 
690 1 0 |a MESSENGER RNA 
690 1 0 |a PHOSPHOGLYCERATE KINASE 
690 1 0 |a PROTOZOAL PROTEIN 
690 1 0 |a PYRUVIC ACID 
690 1 0 |a RNA BINDING PROTEIN 
690 1 0 |a URACIL 
690 1 0 |a VARIANT SURFACE GLYCOPROTEIN 
690 1 0 |a ARTICLE 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a DISEASE TRANSMISSION 
690 1 0 |a EUKARYOTE 
690 1 0 |a EVOLUTION 
690 1 0 |a GLYCOLYSIS 
690 1 0 |a GROWTH INHIBITION 
690 1 0 |a MITOCHONDRION 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN EXPRESSION 
690 1 0 |a PROTEIN RNA BINDING 
690 1 0 |a PROTEIN STABILITY 
690 1 0 |a RNA STABILITY 
690 1 0 |a RNA STRUCTURE 
690 1 0 |a RNA SYNTHESIS 
690 1 0 |a TRYPANOSOMA 
690 1 0 |a TRYPANOSOMA BRUCEI 
690 1 0 |a TSETSE FLY 
690 1 0 |a 3' UNTRANSLATED REGIONS 
690 1 0 |a ADENINE 
690 1 0 |a ANIMALS 
690 1 0 |a ANTIGENS, SURFACE 
690 1 0 |a BASE SEQUENCE 
690 1 0 |a GENE EXPRESSION REGULATION, DEVELOPMENTAL 
690 1 0 |a HUMANS 
690 1 0 |a MOLECULAR SEQUENCE DATA 
690 1 0 |a PHOSPHOGLYCERATE KINASE 
690 1 0 |a PROTOZOAN PROTEINS 
690 1 0 |a REGULATORY SEQUENCES, NUCLEIC ACID 
690 1 0 |a RNA STABILITY 
690 1 0 |a RNA, MESSENGER 
690 1 0 |a RNA, PROTOZOAN 
690 1 0 |a RNA-BINDING PROTEINS 
690 1 0 |a TRYPANOSOMA BRUCEI BRUCEI 
690 1 0 |a URACIL 
690 1 0 |a EUKARYOTA 
690 1 0 |a GLOSSINA (PROPER) 
690 1 0 |a MAMMALIA 
690 1 0 |a PROTOZOA 
690 1 0 |a TRYPANOSOMA 
690 1 0 |a TRYPANOSOMA BRUCEI 
700 1 |a Guerra-Giraldez, C. 
700 1 |a Drozdz, M. 
700 1 |a Hartmann, C. 
700 1 |a Irmer, H. 
700 1 |a Ben-Dov, C. 
700 1 |a Cristodero, M. 
700 1 |a Ding, M. 
700 1 |a Clayton, C. 
773 0 |d 2002  |g v. 30  |h pp. 4414-4424  |k n. 20  |p Nucleic Acids Res.  |x 03051048  |w (AR-BaUEN)CENRE-1769  |t Nucleic Acids Research 
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856 4 0 |u https://hdl.handle.net/20.500.12110/paper_03051048_v30_n20_p4414_Quijada  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03051048_v30_n20_p4414_Quijada  |y Registro en la Biblioteca Digital 
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