Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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

Genetics | Jun 4, 2013

http://www.ncbi.nlm.nih.gov/pubmed/23525333

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.

Pubmed ID: 23525333 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Chromosomal Proteins, Non-Histone | Chromosome Segregation | DNA-Binding Proteins | Mutation | Protein Structure, Tertiary | Proteolysis | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Ubiquitination

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: Intramural NIH HHS, Id:

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.