Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/53308
COMPARTIR / EXPORTAR:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invitar a revisión por pares abierta
Título

Intron retention in the Drosophila melanogaster Rieske iron sulphur protein gene generated a new protein

AutorGontijo, Alisson M. CSIC; Miguela, Verónica CSIC; Whiting, Michael F.; Woodruff, R. C.; Domínguez, María CSIC ORCID
Fecha de publicación2011
EditorNature Publishing Group
CitaciónNature Communications 2(1): 323 (2011)
ResumenGenomes can encode a variety of proteins with unrelated architectures and activities. It is known that protein-coding genes of de novo origin have significantly contributed to this diversity. However, the molecular mechanisms and evolutionary processes behind these originations are still poorly understood. Here we show that the last 102 codons of a novel gene, Noble, assembled directly from non-coding DNA following an intronic deletion that induced alternative intron retention at the Drosophila melanogaster Rieske Iron Sulphur Protein (RFeSP) locus. A systematic analysis of the evolutionary processes behind the origin of Noble showed that its emergence was strongly biased by natural selection on and around the RFeSP locus. Noble mRNA is shown to encode a bona fide protein that lacks an iron sulphur domain and localizes to mitochondria. Together, these results demonstrate the generation of a novel protein at a naturally selected site. © 2011 Macmillan Publishers Limited. All rights reserved.
URIhttp://hdl.handle.net/10261/53308
DOI10.1038/ncomms1328
Identificadoresdoi: 10.1038/ncomms1328
issn: 2041-1723
Aparece en las colecciones: (IN) Artículos




Ficheros en este ítem:
Fichero Descripción Tamaño Formato
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo

CORE Recommender

PubMed Central
Citations

18
checked on 19-abr-2024

SCOPUSTM   
Citations

26
checked on 17-abr-2024

WEB OF SCIENCETM
Citations

22
checked on 27-feb-2024

Page view(s)

325
checked on 22-abr-2024

Download(s)

110
checked on 22-abr-2024

Google ScholarTM

Check

Altmetric

Altmetric


Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.