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Functional conservation of Dhh1p, a cytoplasmic DExD/H-box protein present in large complexes.
Tseng-Rogenski, Stephanie S-I; Chong, Jean-Leon; Thomas, Christopher B; Enomoto, Shinichiro; Berman, Judith; Chang, Tien-Hsien.
Afiliación
  • Tseng-Rogenski SS; Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.
Nucleic Acids Res ; 31(17): 4995-5002, 2003 Sep 01.
Article en En | MEDLINE | ID: mdl-12930949
ABSTRACT
The DHH1 gene in the yeast Saccharomyces cerevisiae encodes a putative RNA helicase of remarkable sequence similarity to several other DExD/H-box proteins, including Xp54 in Xenopus laevis and Ste13p in Schizosaccharomyces pombe. We show here that over-expression of Xp54, an integral component of the stored messenger ribonucleoprotein (mRNP) particles, can rescue the loss of Dhh1p in yeast. Localization and sedimentation studies showed that Dhh1p exists predominantly in the cytoplasm and is present in large complexes whose sizes appear to vary according to the growth stage of the cell culture. In addition, deletion of dhh1, when placed in conjunction with the mutant dbp5 and ded1 alleles, resulted in a synergistically lethal effect, suggesting that Dhh1p may have a role in mRNA export and translation. Finally, similar to Ste13p, Dhh1p is required for sporulation in the budding yeast. Taken together, our data provide evidence that the functions of Dhh1p are conserved through evolution.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteínas de Unión al ARN / ARN Helicasas / Proteínas de Schizosaccharomyces pombe Idioma: En Revista: Nucleic Acids Res Año: 2003 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteínas de Unión al ARN / ARN Helicasas / Proteínas de Schizosaccharomyces pombe Idioma: En Revista: Nucleic Acids Res Año: 2003 Tipo del documento: Article País de afiliación: Estados Unidos