Molecular Biology of the Cell Sign up for new MBC in Press e-TOCs!

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print September 29, 2004
Mol. Biol. Cell 10.1091/mbc.E04-07-0608

A more recent version of this article appeared on December 1, 2004
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E04-07-0608v1
15/12/5443    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lee, S.-J.
Right arrow Articles by Stern, D. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lee, S.-J.
Right arrow Articles by Stern, D. F.

Submitted on July 20, 2004
Revised on September 17, 2004
Accepted on September 20, 2004

A Ddc2-Rad53 Fusion Protein Can Bypass the Requirements for RAD9 and MRC1 in Rad53 Activation

Soo-Jung Lee,* Jimmy K. Duong,{dagger} and David F. Stern{dagger}{ddagger}

{dagger}Department of Pathology, Yale University School of Medicine, New Haven, CT 06510; *Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94107

Monitoring Editor: Douglas Koshland

Activation of Rad53p by DNA damage plays an essential role in DNA damage checkpoint pathways. Rad53p activation requires coupling of Rad53p to Mec1p through a "mediator" protein, Rad9p or Mrc1p. We sought to determine whether the mediator requirement could be circumvented by making fusion proteins between the Mec1 binding partner Ddc2p and Rad53p. Ddc2-Rad53p interacted with Mec1p and other Ddc2-Rad53p molecules under basal conditions, and displayed an increased oligomerization upon DNA damage. Ddc2-Rad53p was activated in a Mec1p- and Tel1p- dependent manner upon DNA damage. Expression of Ddc2-Rad53p in {Delta}rad9 or {Delta}rad9{Delta}mrc1 cells increased viability on plates containing the alkylating agent methyl methane sulfonate (MMS). Ddc2-Rad53p was activated at least partially by DNA damage in {Delta}rad9{Delta}mrc1 cells. In addition, expression of Ddc2-Rad53p in {Delta}rad24{Delta}rad17{Delta}mec3 cells increased cell survival. These results reveal minimal requirements for function of a core checkpoint signaling system.

{ddagger}Corresponding author. E-mail: df.stern{at}yale.edu




This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
H. Cartagena-Lirola, I. Guerini, N. Manfrini, G. Lucchini, and M. P. Longhese
Role of the Saccharomyces cerevisiae Rad53 Checkpoint Kinase in Signaling Double-Strand Breaks during the Meiotic Cell Cycle
Mol. Cell. Biol., July 15, 2008; 28(14): 4480 - 4493.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Javaheri, R. Wysocki, O. Jobin-Robitaille, M. Altaf, J. Cote, and S. J. Kron
Yeast G1 DNA damage checkpoint regulation by H2A phosphorylation is independent of chromatin remodeling
PNAS, September 12, 2006; 103(37): 13771 - 13776.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J.-L. Ma, S.-J. Lee, J. K. Duong, and D. F. Stern
Activation of the Checkpoint Kinase Rad53 by the Phosphatidyl Inositol Kinase-like Kinase Mec1
J. Biol. Chem., February 17, 2006; 281(7): 3954 - 3963.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
R. Wysocki, A. Javaheri, S. Allard, F. Sha, J. Cote, and S. J. Kron
Role of Dot1-Dependent Histone H3 Methylation in G1 and S Phase DNA Damage Checkpoint Functions of Rad9
Mol. Cell. Biol., October 1, 2005; 25(19): 8430 - 8443.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2004 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.