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Sanchez, S.E.; Petrillo, E.; Beckwith, E.J.; Zhang, X.; Rugnone, M.L.; Hernando, C.E.; Cuevas, J.C.; Godoy Herz, M.A.; Depetris-Chauvin, A.; Simpson, C.G.; Brown, J.W.S.; Cerdán, P.D.; Borevitz, J.O.; Mas, P.; Ceriani, M.F.; Kornblihtt, A.R.; Yanovsky, M.J. "A methyl transferase links the circadian clock to the regulation of alternative splicing" (2010) Nature. 468(7320):112-116
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Abstract:

Circadian rhythms allow organisms to time biological processes to the most appropriate phases of the dayg-night cycle. Post-transcriptional regulation is emerging as an important component of circadian networks, but the molecular mechanisms linking the circadian clock to the control of RNA processing are largely unknown. Here we show that PROTEIN ARGININE METHYL TRANSFERASE 5 (PRMT5), which transfers methyl groups to arginine residues present in histones and Sm spliceosomal proteins, links the circadian clock to the control of alternative splicing in plants. Mutations in PRMT5 impair several circadian rhythms in Arabidopsis thaliana and this phenotype is caused, at least in part, by a strong alteration in alternative splicing of the core-clock gene PSEUDO RESPONSE REGULATOR 9 (PRR9). Furthermore, genome-wide studies show that PRMT5 contributes to the regulation of many pre-messenger-RNA splicing events, probably by modulating 5ĝ€2-splice-site recognition. PRMT5 expression shows daily and circadian oscillations, and this contributes to the mediation of the circadian regulation of expression and alternative splicing of a subset of genes. Circadian rhythms in locomotor activity are also disrupted in dart5-1, a mutant affected in the Drosophila melanogaster PRMT5 homologue, and this is associated with alterations in splicing of the core-clock gene period and several clock-associated genes. Our results demonstrate a key role for PRMT5 in the regulation of alternative splicing and indicate that the interplay between the circadian clock and the regulation of alternative splicing by PRMT5 constitutes a common mechanism that helps organisms to synchronize physiological processes with daily changes in environmental conditions. © 2010 Macmillan Publishers Limited. All rights reserved.

Registro:

Documento: Artículo
Título:A methyl transferase links the circadian clock to the regulation of alternative splicing
Autor:Sanchez, S.E.; Petrillo, E.; Beckwith, E.J.; Zhang, X.; Rugnone, M.L.; Hernando, C.E.; Cuevas, J.C.; Godoy Herz, M.A.; Depetris-Chauvin, A.; Simpson, C.G.; Brown, J.W.S.; Cerdán, P.D.; Borevitz, J.O.; Mas, P.; Ceriani, M.F.; Kornblihtt, A.R.; Yanovsky, M.J.
Filiación:IFEVA, Facultad de Agronomía, UBA-CONICET, C1417DSE Buenos Aires, Argentina
IFIBYNE, FCEyN, UBA-CONICET, C1428EGA Buenos Aires, Argentina
Fundación Instituto Leloir, IIBBA-CONICET, C1405BWEBuenos Aires, Argentina
Department of Ecology and Evolution, University of Chicago, Chicago, IL 60637, United States
Centre for Research in Agricultural Genomics (CRAG), Consortium CSIC-IRTAUAB, Barcelona 08034, Spain
Genetics Programme, SCRI, Dundee DD2 5DA, United Kingdom
Division of Plant Sciences, University of Dundee at SCRI, Dundee, DD2 5DA, United Kingdom
Palabras clave:arginine derivative; histone; methyl group; methyltransferase; protein arginine methyltransferase; protein arginine methyltransferase 5; protein Sm; pseudo response regulator 9; regulator protein; RNA; unclassified drug; circadian rhythm; enzyme activity; fly; gene expression; genetic analysis; genome; physiological response; alternative RNA splicing; Arabidopsis; article; circadian rhythm; controlled study; Drosophila melanogaster; gene disruption; gene mutation; gene overexpression; locomotion; molecular clock; molecular recognition; nonhuman; oscillation; phenotype; priority journal; protein expression; Alternative Splicing; Animals; Arabidopsis; Arabidopsis Proteins; Base Sequence; Circadian Clocks; Circadian Rhythm; Darkness; Drosophila melanogaster; Drosophila Proteins; Gene Expression Profiling; Gene Expression Regulation, Plant; Light; Methylation; Mutation; Period Circadian Proteins; Phenotype; Protein Methyltransferases; Protein-Arginine N-Methyltransferases; RNA Precursors; RNA Splice Sites; RNA, Messenger; Spliceosomes; Transcription Factors; Arabidopsis thaliana; Drosophila melanogaster
Año:2010
Volumen:468
Número:7320
Página de inicio:112
Página de fin:116
DOI: http://dx.doi.org/10.1038/nature09470
Título revista:Nature
Título revista abreviado:Nature
ISSN:00280836
CODEN:NATUA
CAS:RNA, 63231-63-0; histone, 9062-68-4; methyltransferase, 9033-25-4; Arabidopsis Proteins; Dart5 protein, Drosophila, 2.1.1.-; Drosophila Proteins; PER protein, Drosophila; PRMT5 protein, Arabidopsis, 2.1.1.23; PRR9 protein, Arabidopsis; Period Circadian Proteins; Protein Methyltransferases, 2.1.1.-; Protein-Arginine N-Methyltransferases, 2.1.1.-; RNA Precursors; RNA Splice Sites; RNA, Messenger; Transcription Factors
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00280836_v468_n7320_p112_Sanchez

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Citas:

---------- APA ----------
Sanchez, S.E., Petrillo, E., Beckwith, E.J., Zhang, X., Rugnone, M.L., Hernando, C.E., Cuevas, J.C.,..., Yanovsky, M.J. (2010) . A methyl transferase links the circadian clock to the regulation of alternative splicing. Nature, 468(7320), 112-116.
http://dx.doi.org/10.1038/nature09470
---------- CHICAGO ----------
Sanchez, S.E., Petrillo, E., Beckwith, E.J., Zhang, X., Rugnone, M.L., Hernando, C.E., et al. "A methyl transferase links the circadian clock to the regulation of alternative splicing" . Nature 468, no. 7320 (2010) : 112-116.
http://dx.doi.org/10.1038/nature09470
---------- MLA ----------
Sanchez, S.E., Petrillo, E., Beckwith, E.J., Zhang, X., Rugnone, M.L., Hernando, C.E., et al. "A methyl transferase links the circadian clock to the regulation of alternative splicing" . Nature, vol. 468, no. 7320, 2010, pp. 112-116.
http://dx.doi.org/10.1038/nature09470
---------- VANCOUVER ----------
Sanchez, S.E., Petrillo, E., Beckwith, E.J., Zhang, X., Rugnone, M.L., Hernando, C.E., et al. A methyl transferase links the circadian clock to the regulation of alternative splicing. Nature. 2010;468(7320):112-116.
http://dx.doi.org/10.1038/nature09470