Regulation of H2B Monoubiquitylation by RNP Recycling Protein Prp24 Public Deposited

Downloadable Content

Download PDF
Last Modified
  • March 21, 2019
Creator
  • Bolling, Katie
    • Affiliation: School of Medicine, Curriculum in Genetics and Molecular Biology
Abstract
  • Post-translational modification of histone proteins and splicing of pre-mRNA transcripts are two fundamental aspects of gene regulation that are essential for eukaryotic life. Often, these processes are investigated in isolation; however, they do not occur independently. Although evidence supports cross-regulation between chromatin and RNA processing, there remains a gap in understanding of the mechanisms involved. Here, I describe a novel function for splicing protein Prp24, mutation of which alters monoubiquitylation of histone H2B (H2Bub1). Whereas the role of Prp24 in spliceosome assembly and recycling has been well studied, it has not been previously associated with a role in chromatin modification. My results indicate that a highly conserved region of Prp24 may be critical for regulating levels of H2Bub1. Investigations into the effects of U6 small nuclear (sn)RNA on this regulation are also discussed. Together, these data suggest a mechanism by which spliceosomal machinery regulates histone modification.
Date of publication
Keyword
DOI
Resource type
Rights statement
  • In Copyright
Advisor
  • Strahl, Brian
  • Hathaway, Nathaniel
  • Matera, Arnold
Degree
  • Master of Science
Degree granting institution
  • University of North Carolina at Chapel Hill Graduate School
Graduation year
  • 2016
Language
Parents:

This work has no parents.

Items