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Evolutionary complementation for polymerase II CTD function.

J W Stiller1, B L McConaughy, B D Hall

  • 1Department of Genetics, University of Washington, Seattle, WA 98195, USA. stiller@u.washington.edu

Yeast (Chichester, England)
|January 6, 2000
PubMed
Summary
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The C-terminal domain (CTD) of eukaryotic RNA polymerase II can tolerate evolutionary variations. Substituting yeast CTD with a protist variant revealed functional insights into CTD evolution and function.

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • The C-terminal domain (CTD) of eukaryotic RNA polymerase II largest subunit (RPB1) is crucial for mRNA transcription.
  • The CTD comprises conserved tandemly repeated heptapeptides, but variations exist across eukaryotes.
  • The functional and evolutionary significance of CTD variations remains largely unexplored.

Purpose of the Study:

  • To investigate the functional and evolutionary implications of variations in the RPB1 CTD.
  • To assess the viability and function of a yeast strain expressing a protist-derived CTD.

Main Methods:

  • Yeast cells were transformed with a construct replacing the wild-type yeast RPB1 CTD with 25 heptads from Mastigamoeba invertens.
  • The Mastigamoeba CTD heptads feature alanine substitutions at positions 4 and 7, differing from the canonical CTD sequence.

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Main Results:

  • The yeast mutants expressing the Mastigamoeba CTD were viable.
  • Mutant viability was observed even under temperature and nutrient stress conditions.
  • These findings highlight the functional tolerance of certain CTD residues.

Conclusions:

  • The study provides novel insights into the functional importance of conserved CTD residues.
  • Expression of evolutionary CTD variants in yeast offers a valuable model for studying CTD origin, evolution, and function.