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Noncanonical CTD kinases regulate RNA polymerase II in a gene-class-specific manner.

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New kinases phosphorylate RNA polymerase II's carboxyl-terminal domain (CTD) at Thr4. This modification, particularly by Hrr25 kinase, is crucial for terminating specific noncoding RNA genes.

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Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Biochemistry

Background:

  • The carboxyl-terminal domain (CTD) of RNA polymerase II (Pol II) is extensively phosphorylated.
  • CTD phosphorylation patterns regulate transcription by recruiting specific protein factors.
  • While Ser7, Ser5, and Ser2 phosphorylations are common, Thr4 phosphorylation's role is less understood.

Purpose of the Study:

  • To identify kinases that phosphorylate Thr4 on the Pol II CTD.
  • To investigate the function of Thr4 phosphorylation in gene transcription.
  • To elucidate the role of Hrr25 kinase in transcription termination.

Main Methods:

  • Kinase screening to identify Thr4 kinases.
  • Chemical inhibition of Hrr25 kinase.
  • Genome-wide profiling of Hrr25.
  • Analysis of transcription termination defects in noncoding genes.

Main Results:

  • Ten novel Thr4 kinases were identified.
  • Hrr25 was identified as a key Thr4 kinase.
  • Inhibition of Hrr25 caused termination defects in specific noncoding snoRNA genes.
  • Hrr25 selectively localizes to the 3' regions of genes with termination issues.
  • Phospho-Thr4 marks are recognized by the termination factor Rtt103.

Conclusions:

  • Uncommon CTD kinases, including Hrr25, place phospho-Thr4 marks.
  • Phospho-Thr4 is essential for the transcription termination of specific noncoding genes.
  • Hrr25-mediated Thr4 phosphorylation regulates gene expression through termination control.