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Absence of Dbp2p alters both nonsense-mediated mRNA decay and rRNA processing

A T Bond1, D A Mangus, F He

  • 1Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655-0122, USA.

Molecular and Cellular Biology
|October 5, 2001
PubMed

Insights

Dbp2p, a DEAD-box protein, aids in nonsense-mediated mRNA decay and rRNA processing by interacting with Upf1p. This dual role is crucial for cellular function, with human p68 partially rescuing its mRNA decay defect.

Area of Science:

  • Molecular Biology
  • Yeast Genetics
  • RNA Metabolism

Background:

  • Dbp2p is a yeast DEAD-box protein homologous to human p68.
  • Upf1p is an essential protein in the nonsense-mediated mRNA decay (NMD) pathway.
  • The interaction domains of Upf1p with Nmd2p and Sup35/45p are known.

Purpose of the Study:

  • To investigate the role of Dbp2p in the nonsense-mediated mRNA decay pathway.
  • To explore Dbp2p's function in ribosome biogenesis and rRNA processing.
  • To elucidate the mechanism by which Dbp2p influences both mRNA decay and rRNA processing.

Main Methods:

  • Investigated Dbp2p:Upf1p interaction using yeast genetics.
  • Analyzed the effect of DBP2 deletion and mutations on nonsense-containing transcript abundance.
  • Examined polyribosome profiles and rRNA processing in Dbp2p-deficient cells.
  • Assessed complementation of Dbp2p functions by human p68.

Main Results:

  • Dbp2p interacts with Upf1p in a region distinct from known interaction domains.
  • Deletion or mutation of DBP2 increases nonsense-containing transcripts, indicating an NMD role.
  • Dbp2p deficiency leads to reduced 60S ribosomal subunits and 25S rRNA, impacting ribosome biogenesis.
  • Human p68 can complement the mRNA decay function but not the rRNA processing defect of dbp2Delta cells.

Conclusions:

  • Dbp2p functions in both nonsense-mediated mRNA decay and rRNA processing.
  • Dbp2p likely alters rRNA structure to facilitate specific processing events and translation termination.
  • Dbp2p's dual role suggests a unifying mechanism involving structural modulation of rRNA.

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