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Structurally conserved and functionally divergent yeast Ssu72 phosphatases.

Ana M Rodríguez-Torres1, Mónica Lamas-Maceiras, Rosa García-Díaz

  • 1Area de Bioquímica, Facultad de Ciencias, Universidade da Coruña (UDC), A Coruña, Spain.

FEBS Letters
|July 9, 2013
PubMed
Summary
This summary is machine-generated.

The eukaryotic Ssu72 factor regulates RNA polymerase II's carboxy-terminal domain (CTD) phosphorylation. Kluyveromyces lactis Ssu72 (KlSsu72) expression in Saccharomyces cerevisiae impairs CTD serine5-P phosphatase activity, affecting RNA processing.

Keywords:
5-fluoro-orotic acidCTDCTD-phosphataseFOAGSTOD(600)RNA polymerase IIRNA polymerase-IIRNA-processingRNAPIISSU72Ser2, Ser5Yeastcarboxy-terminal domain (CTD) of the major subunit of RNA polymerase IIglutathione S-transferaseoptical density at 600 nanometerspNPPparanitrophenylphosphateserine 2 and 5, respectively, from CTD repeats

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • The Ssu72 factor is a key eukaryotic protein involved in various RNA biogenesis pathways.
  • Ssu72 possesses phosphatase activity targeting the carboxy-terminal domain (CTD) of RNA polymerase II's largest subunit.
  • Understanding Ssu72's precise role is crucial for comprehending gene expression regulation.

Purpose of the Study:

  • To investigate the phosphatase activity of Kluyveromyces lactis Ssu72 (KlSsu72).
  • To determine the functional impact of KlSsu72 expression in Saccharomyces cerevisiae, specifically on CTD phosphorylation.
  • To explore the relationship between Ssu72 function, CTD serine5-P levels, and alternative 3'-end RNA processing.

Main Methods:

  • In vitro phosphatase assays using pNPP substrate to characterize KlSsu72 activity.
  • Expression of KlSsu72 in Saccharomyces cerevisiae to assess its in vivo effects.
  • Analysis of CTD serine5-P levels under different growth conditions.
  • Investigation of RNA14 alternative 3'-end processing events.

Main Results:

  • KlSsu72 demonstrated in vitro phosphatase activity inhibited by ortho-vanadate.
  • Expression of KlSsu72 in Saccharomyces cerevisiae resulted in defective CTD serine5-P phosphatase activity.
  • Ssu72 was confirmed as essential for maintaining normal CTD serine5-P levels during specific growth phases.
  • Significant alterations in RNA14 alternative 3'-end processing were observed, independent of CTD serine5-P levels.

Conclusions:

  • KlSsu72 exhibits conserved phosphatase activity crucial for RNA polymerase II CTD regulation.
  • Ssu72 plays a vital role in maintaining appropriate CTD serine5-P homeostasis.
  • The study highlights a potential Ssu72-mediated pathway influencing alternative RNA processing distinct from CTD phosphorylation effects.