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Related Experiment Videos

The DECD box putative ATPase Sub2p is an early mRNA export factor.

T H Jensen1, J Boulay, M Rosbash

  • 1Howard Hughes Medical Institute, Department of Biology, Brandeis University, Waltham, MA 02454, USA. thj@mbio.aau.dk

Current Biology : CB
|November 7, 2001
PubMed
Summary

The DECD box ATPase Sub2p (UAP56) is crucial for nuclear mRNA export in Saccharomyces cerevisiae. Mutant strains show significant nuclear accumulation of poly(A)(+) RNA, indicating a general role beyond splicing.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • Nuclear mRNA metabolism involves transcription, processing, and export.
  • RNA polymerase II transcripts undergo significant nuclear rearrangements.
  • RNA helicases/ATPases are essential for mRNP remodeling during mRNA processing and export.

Purpose of the Study:

  • To investigate the function of the DECD box RNA-dependent ATPase Sub2p (UAP56) in Saccharomyces cerevisiae.
  • To determine the role of Sub2p in nuclear mRNA metabolism and export.
  • To explore the relationship between Sub2p, splicing, and other nuclear factors.

Main Methods:

  • Analysis of poly(A)(+) RNA localization in yeast strains with mutant sub2 alleles.
  • Examination of intronless HSP104 transcript nuclear accumulation.

Related Experiment Videos

  • Investigation of genetic and functional interactions between Sub2p, Rad3p, and Rrp6p.
  • Main Results:

    • Mutant alleles of sub2 lead to rapid and dramatic nuclear accumulation of poly(A)(+) RNA.
    • An intronless transcript (HSP104) also accumulates in the nucleus, suggesting a role beyond splicing.
    • Sub2p interacts genetically and functionally with Rad3p and Rrp6p, implicating it in mRNA export pathways.

    Conclusions:

    • Sub2p (UAP56) plays a general role in nuclear mRNA export, not limited to splicing.
    • Sub2p functions at an early step in the mRNA export process.
    • Interactions with Rad3p and Rrp6p highlight Sub2p's integration into mRNA processing and export machinery.