Nucleic Acids Research, 2003, Vol. 31, No. 17 4995-5002
© 2003 Oxford University Press
Functional conservation of Dhh1p, a cytoplasmic DExD/H-box protein present in large complexes
Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA and 1 Department of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, MN 55455, USA
*To whom correspondence should be addressed. Tel: +1 614 688 8678; Fax: +1 614 292 4466; Email: chang.108{at}osu.edu
Present addresses:
Stephanie S.-I Tseng-Rogenski, Department of Urology, School of Medicine, University of Michigan, Ann Arbor, MI 48109, USA
Christopher B. Thomas, Department of Medicine, The Ohio State University, Columbus, OH 43210, USA
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.
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