MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Edwards, S.
Right arrow Articles by Campbell, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Edwards, S.
Right arrow Articles by Campbell, J. L.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, April 2003, p. 2733-2748, Vol. 23, No. 8
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.8.2733-2748.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Saccharomyces cerevisiae DNA Polymerase {varepsilon} and Polymerase {sigma} Interact Physically and Functionally, Suggesting a Role for Polymerase {varepsilon} in Sister Chromatid Cohesion

Shaune Edwards, Caroline M. Li, Daniel L. Levy, Jessica Brown,{dagger} Peter M. Snow, and Judith L. Campbell*

Braun Laboratories, California Institute of Technology, Pasadena, California 91125

Received 16 August 2002/ Returned for modification 25 September 2002/ Accepted 16 January 2003

The large subunit of Saccharomyces cerevisiae DNA polymerase {varepsilon}, Pol2, comprises two essential functions. The N terminus has essential DNA polymerase activity. The C terminus is also essential, but its function is unknown. We report here that the C-terminal domain of Pol2 interacts with polymerase {sigma} (Pol {sigma}), a recently identified, essential nuclear nucleotidyl transferase encoded by two redundant genes, TRF4 and TRF5. This interaction is functional, since Pol {sigma} stimulates the polymerase activity of the Pol {varepsilon} holoenzyme significantly. Since Trf4 is required for sister chromatid cohesion as well as for completion of S phase and repair, the interaction suggested that Pol {varepsilon}, like Pol {sigma}, might form a link between the replication apparatus and sister chromatid cohesion and/or repair machinery. We present evidence that pol2 mutants are defective in sister chromatid cohesion. In addition, Pol2 interacts with SMC1, a subunit of the cohesin complex, and with ECO1/CTF7, required for establishing sister chromatid cohesion; and pol2 mutations act synergistically with smc1 and scc1. We also show that trf5{Delta} mutants, like trf4{Delta} mutants, are defective in DNA repair and sister chromatid cohesion.

* Corresponding author. Mailing address: Braun Laboratories 147-75, California Institute of Technology, Pasadena, CA 91125. Phone: (626) 395-6053. Fax: (626) 405-9452. E-mail: jcampbel{at}its.caltech.edu.

{dagger} Present address: Department of Biochemistry and Biophysics, University of San Francisco, San Francisco, CA 94143.

Molecular and Cellular Biology, April 2003, p. 2733-2748, Vol. 23, No. 8
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.8.2733-2748.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2003 by the American Society for Microbiology. All rights reserved.