JCB logo
R&D Systems
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online November 26, 2007
doi:10.1083/jcb.200706040
The Journal of Cell Biology, Vol. 179, No. 5, 845-854
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Bupp et al.
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bupp, J. M.
Right arrow Articles by Jaspersen, S. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bupp, J. M.
Right arrow Articles by Jaspersen, S. L.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

 Telomere anchoring at the nuclear periphery requires the budding yeast Sad1-UNC-84 domain protein Mps3

Jennifer M. Bupp1, Adriana E. Martin1, Elizabeth S. Stensrud1, and Sue L. Jaspersen1,2

1 Stowers Institute for Medical Research, Kansas City, MO 64110
2 Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160

Correspondence to S.L. Jaspersen: slj{at}stowers-institute.org

Positioning of telomeres at the nuclear periphery can have dramatic effects on gene expression by establishment of heritable, transcriptionally repressive subdomains. However, little is known about the integral membrane proteins that mediate telomere tethering at the nuclear envelope. Here, we find a previously unrecognized function for the Saccharomyces cerevisiae Sad1-UNC-84 domain protein Mps3 in regulating telomere positioning in mitotic cells. Our data demonstrate that the nucleoplasmic N-terminal acidic domain of Mps3 is not essential for viability. However, this acidic domain is necessary and sufficient for telomere tethering during S phase and the silencing of reporter constructs integrated at telomeres. We show that this is caused by the role of the Mps3 acidic domain in binding and localization of the silent information regulator protein Sir4 to the nuclear periphery. Thus, Mps3 functions as an integral membrane anchor for telomeres and is a novel nuclear receptor for the Sir4 pathway of telomere tethering and gene inactivation.

J.M. Bupp and A.E. Martin contributed equally to this paper.

Abbreviations used in this paper: 5-FOA, 5-fluoroorotic acid; LacOR, lactose operator; lexAop, LexA operators; rDNA, ribosomal DNA; SIR, silent information regulator; SPB, spindle pole body; SUN, Sad1-UNC-84.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents