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Utp14 interaction with the small subunit processome.

Joshua J Black1, Zhaohui Wang1, Lisa M Goering2

  • 1Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas 78712, USA.

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|June 22, 2018
PubMed
Summary
This summary is machine-generated.

The protein Utp14 is crucial for small ribosomal subunit biogenesis, controlling RNA helicase Dhr1 activity and facilitating the transition to pre-40S particles. It also aids in recruiting the RNA exosome for efficient ribosome assembly.

Keywords:
40SSSU processomeUtp14exosome

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The SSU processome (90S) is a key intermediate in eukaryotic small ribosomal subunit biogenesis.
  • Transition to pre-40S particles requires RNA compaction and release of biogenesis factors, including U3 snoRNA.
  • The RNA helicase Dhr1 and Utp14 protein are implicated in U3 release and subsequent steps.

Purpose of the Study:

  • To investigate the role of Utp14 in controlling Dhr1 activity and its interaction with the SSU processome.
  • To characterize the molecular mechanisms by which Utp14 regulates ribosome biogenesis.
  • To determine Utp14's function in the recruitment of other factors, such as the RNA exosome.

Main Methods:

  • UV crosslinking and analysis of cDNA (CRAC) to map Utp14 interactions.
  • Yeast two-hybrid assays to identify Utp14 binding partners.
  • Proteomic analysis of SSU particles lacking Utp14.

Main Results:

  • Utp14 interacts with the preribosome, although it lacks recognizable domains.
  • Utp14 is essential for the efficient recruitment of the RNA exosome to SSU particles.
  • The study provides insights into how Utp14 communicates assembly status within the SSU processome.

Conclusions:

  • Utp14 acts as a critical regulator in small ribosomal subunit biogenesis, linking RNA helicase activity to ribosome assembly status.
  • Utp14's function is vital for the timely release of U3 snoRNA and the transition to pre-40S particles.
  • Utp14 plays a central role in coordinating multiple steps of ribosome assembly, including exosome recruitment.