Your browser doesn't support javascript.
loading
Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subunit of the PAQosome.
Cloutier, Philippe; Poitras, Christian; Faubert, Denis; Bouchard, Annie; Blanchette, Mathieu; Gauthier, Marie-Soleil; Coulombe, Benoit.
Afiliación
  • Cloutier P; Institut de Recherches Cliniques de Montréal , 110 Avenue des Pins Ouest , Montréal , Quebec H2W 1R7 , Canada.
  • Poitras C; Institut de Recherches Cliniques de Montréal , 110 Avenue des Pins Ouest , Montréal , Quebec H2W 1R7 , Canada.
  • Faubert D; Institut de Recherches Cliniques de Montréal , 110 Avenue des Pins Ouest , Montréal , Quebec H2W 1R7 , Canada.
  • Bouchard A; Institut de Recherches Cliniques de Montréal , 110 Avenue des Pins Ouest , Montréal , Quebec H2W 1R7 , Canada.
  • Blanchette M; School of Computer Science , McGill University , 3480 University Street , Montréal , Quebec H3A 0E9 , Canada.
  • Gauthier MS; Institut de Recherches Cliniques de Montréal , 110 Avenue des Pins Ouest , Montréal , Quebec H2W 1R7 , Canada.
  • Coulombe B; Institut de Recherches Cliniques de Montréal , 110 Avenue des Pins Ouest , Montréal , Quebec H2W 1R7 , Canada.
J Proteome Res ; 19(1): 18-27, 2020 01 03.
Article en En | MEDLINE | ID: mdl-31738558
ABSTRACT
The PAQosome is an 11-subunit chaperone involved in the biogenesis of several human protein complexes. We show that ASDURF, a recently discovered upstream open reading frame (uORF) in the 5' UTR of ASNSD1 mRNA, encodes the 12th subunit of the PAQosome. ASDURF displays significant structural homology to ß-prefoldins and assembles with the five known subunits of the prefoldin-like module of the PAQosome to form a heterohexameric prefoldin-like complex. A model of the PAQosome prefoldin-like module is presented. The data presented here provide an example of a eukaryotic uORF-encoded polypeptide whose function is not limited to cis-acting translational regulation of downstream coding sequence and highlights the importance of including alternative ORF products in proteomic studies.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Chaperonas Moleculares / Proteómica Límite: Humans Idioma: En Revista: J Proteome Res Asunto de la revista: BIOQUIMICA Año: 2020 Tipo del documento: Article País de afiliación: Canadá

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Chaperonas Moleculares / Proteómica Límite: Humans Idioma: En Revista: J Proteome Res Asunto de la revista: BIOQUIMICA Año: 2020 Tipo del documento: Article País de afiliación: Canadá