Format

Send to:

Choose Destination
See comment in PubMed Commons below
Genetics. 2013 Jun;194(2):513-8. doi: 10.1534/genetics.113.149898. Epub 2013 Mar 22.

A novel role of the N terminus of budding yeast histone H3 variant Cse4 in ubiquitin-mediated proteolysis.

Author information

  • 1Genetics Branch Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20889, USA.

Abstract

Regulating levels of centromeric histone H3 (CenH3) variant is crucial for genome stability. Interaction of Psh1, an E3 ligase, with the C terminus of Cse4 has been shown to contribute to its proteolysis. Here, we demonstrate a role for ubiquitination of the N terminus of Cse4 in regulating Cse4 proteolysis for faithful chromosome segregation and a role for Doa1 in ubiquitination of Cse4.

KEYWORDS:

Cse4; Doa1; Psh1; chromosome segregation; ubiquitin-mediated protein degradation

PMID:
23525333
[PubMed - indexed for MEDLINE]
PMCID:
PMC3664860
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk