HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 28, 20388-20394, July 13, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/28/20388    most recent M702652200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kosoy, A. Articles by O'Connell, M. J. Search for Related Content PubMed PubMed Citation Articles by Kosoy, A. Articles by O'Connell, M. J. Social Bookmarking                      What's this?

Fission Yeast Rnf4 Homologs Are Required for DNA Repair^*

From the Department of Oncological Sciences, Mount Sinai School of Medicine, New York, New York 10029

We describe two RING finger proteins in the fission yeast Schizosaccharomyces pombe, Rfp1 and Rfp2. We show that these proteins function redundantly in DNA repair. Rfp1 was isolated as a Chk1-interacting protein in a two-hybrid screen and has high amino acid sequence similarity to Rfp2. Deletion of either gene does not cause a phenotype, but a double deletion (rfp1rfp2) showed poor viability and defects in cell cycle progression. These cells are also sensitive to DNA-damaging agents, although they maintained normal checkpoint signaling to Chk1. Rfp1 and Rfp2 are most closely related to human Rnf4, and we showed that Rnf4 can substitute functionally for Rfp1 and/or Rfp2. The double mutants also showed significantly increased levels of protein SUMOylation, and we identified an S. pombe Ulp2/Smt4 homolog that, when overexpressed, reduced SUMO levels and suppressed the DNA damage sensitivity of rfp1 rfp2 cells.

Received for publication, March 28, 2007 , and in revised form, May 14, 2007.

^* This work was supported by National Institutes of Health/NCI Grant CA100076. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Oncological Sciences, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, NY 10029. Tel.: 212-659-5468; Fax: 212-987-2240; E-mail: matthew.oconnell{at}mssm.edu.

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

This article has been cited by other articles:

				A. Kosoy and M. J. O'Connell Regulation of Chk1 by Its C-terminal Domain Mol. Biol. Cell, November 1, 2008; 19(11): 4546 - 4553. [Abstract] [Full Text] [PDF]

				J. R. Mullen and S. J. Brill Activation of the Slx5-Slx8 Ubiquitin Ligase by Poly-small Ubiquitin-like Modifier Conjugates J. Biol. Chem., July 18, 2008; 283(29): 19912 - 19921. [Abstract] [Full Text] [PDF]

				K. Uzunova, K. Gottsche, M. Miteva, S. R. Weisshaar, C. Glanemann, M. Schnellhardt, M. Niessen, H. Scheel, K. Hofmann, E. S. Johnson, et al. Ubiquitin-dependent Proteolytic Control of SUMO Conjugates J. Biol. Chem., November 23, 2007; 282(47): 34167 - 34175. [Abstract] [Full Text] [PDF]

				Y. Xie, O. Kerscher, M. B. Kroetz, H. F. McConchie, P. Sung, and M. Hochstrasser The Yeast Hex3{middle dot}Slx8 Heterodimer Is a Ubiquitin Ligase Stimulated by Substrate Sumoylation J. Biol. Chem., November 23, 2007; 282(47): 34176 - 34184. [Abstract] [Full Text] [PDF]