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Molecular and Cellular Biology, October 2006, p. 7783-7790, Vol. 26, No. 20
0270-7306/06/$08.00+0     doi:10.1128/MCB.01260-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Mms2-Ubc13-Dependent and -Independent Roles of Rad5 Ubiquitin Ligase in Postreplication Repair and Translesion DNA Synthesis in Saccharomyces cerevisiae{triangledown}

Venkateswarlu Gangavarapu,1 Lajos Haracska,1,2 Ildiko Unk,1,2 Robert E. Johnson,1 Satya Prakash,1 and Louise Prakash1*

Sealy Center for Molecular Science, University of Texas Medical Branch, Galveston, Texas,1 Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary2

Received 11 July 2006/ Accepted 2 August 2006

The Rad6-Rad18 ubiquitin-conjugating enzyme complex of Saccharomyces cerevisiae promotes replication through DNA lesions via three separate pathways that include translesion synthesis (TLS) by DNA polymerases {eta} and {zeta} and postreplicational repair (PRR) of discontinuities that form in the newly synthesized DNA opposite from DNA lesions, mediated by the Mms2-Ubc13 ubiquitin-conjugating enzyme and Rad5. Rad5 is an SWI/SNF family ATPase, and additionally, it functions as a ubiquitin ligase in the ubiquitin conjugation reaction. To decipher the roles of these Rad5 activities in lesion bypass, here we examine the effects of mutations in the Rad5 ATPase and ubiquitin ligase domains on the PRR of UV-damaged DNA and on UV-induced mutagenesis. Even though the ATPase-defective mutation confers only a modest degree of UV sensitivity whereas the ubiquitin ligase mutation causes a high degree of UV sensitivity, we find that both of these mutations produce the same high level of PRR defect as that conferred by the highly UV-sensitive rad5{Delta} mutation. From these studies, we infer a requirement of the Rad5 ATPase and ubiquitin ligase activities in PRR, and based upon the effects of different rad5 mutations on UV mutagenesis, we suggest a role for Rad5 in affecting the efficiency of lesion bypass by the TLS polymerases. In contrast to the role of Rad5 in PRR, however, where its function is coupled with that of Mms2-Ubc13, Rad5 function in TLS would be largely independent of this ubiquitin-conjugating enzyme complex.

* Corresponding author. Mailing address: Sealy Center for Molecular Science, University of Texas Medical Branch at Galveston, Galveston, TX 77555-1061. Phone: (409) 747-8601. Fax: (409) 747-8608. E-mail: l.prakash{at}utmb.edu.

{triangledown} Published ahead of print on 14 August 2006.

Molecular and Cellular Biology, October 2006, p. 7783-7790, Vol. 26, No. 20
0270-7306/06/$08.00+0     doi:10.1128/MCB.01260-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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