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Related Experiment Videos

A CTD function linking transcription to splicing

J L Corden1, M Patturajan

  • 1Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. jeff_corden@qmail.bs.jhu.edu

Trends in Biochemical Sciences
|December 16, 1997
PubMed
Summary

The C-terminal domain (CTD) of RNA polymerase II acts as a platform for pre-mRNA processing. New CTD-associated SR-like proteins (CASPs) are involved in this process and transcription elongation.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • The C-terminal domain (CTD) of RNA polymerase II, discovered in 1985, has an enigmatic function.
  • Emerging evidence suggests the CTD serves as a scaffold for the assembly of molecular complexes involved in RNA processing.

Purpose of the Study:

  • To elucidate the role of the CTD in pre-mRNA processing and transcription.
  • To identify novel proteins associated with the CTD and their functions.

Main Methods:

  • The study likely involved biochemical assays to identify CTD-associated proteins.
  • Functional studies to assess the impact of these proteins on pre-mRNA processing and transcription elongation.

Main Results:

  • A novel set of CTD-associated SR-like proteins (CASPs) were identified.

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  • CASPs are implicated in pre-mRNA splicing, cleavage, and polyadenylation.
  • CASPs play a role in transcription elongation as part of the 'transcriptosome'.

    • Conclusions:

    • The CTD is a crucial platform for coordinating multiple steps of pre-mRNA metabolism.
    • CASPs represent a new class of proteins integral to the 'transcriptosome', linking transcription and RNA processing.