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Molecular and Cellular Biology, November 2004, p. 9401-9413, Vol. 24, No. 21
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.21.9401-9413.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Rad62 Protein Functionally and Physically Associates with the Smc5/Smc6 Protein Complex and Is Required for Chromosome Integrity and Recombination Repair in Fission Yeast

Hirofumi Morikawa,1 Takashi Morishita,1 Shiho Kawane,1,{dagger} Hiroshi Iwasaki,1,{ddagger} Antony M. Carr,2 and Hideo Shinagawa1*

Department of Molecular Microbiology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan,1 Genome Damage and Stability Centre, School of Biological Sciences, University of Sussex, Brighton, United Kingdom2

Received 9 April 2004/ Returned for modification 3 May 2004/ Accepted 27 July 2004

Smc5 and Smc6 proteins form a heterodimeric SMC (structural maintenance of chromosome) protein complex like SMC1-SMC3 cohesin and SMC2-SMC4 condensin, and they associate with non-SMC proteins Nse1 and Nse2 stably and Rad60 transiently. This multiprotein complex plays an essential role in maintaining chromosome integrity and repairing DNA double strand breaks (DSBs). This study characterizes a Schizosaccharomyces pombe mutant rad62-1, which is hypersensitive to methyl methanesulfonate (MMS) and synthetically lethal with rad2 (a feature of recombination mutants). rad62-1 is hypersensitive to UV and gamma rays, epistatic with rhp51, and defective in repair of DSBs. rad62 is essential for viability and genetically interacts with rad60, smc6, and brc1. Rad62 protein physically associates with the Smc5-6 complex. rad62-1 is synthetically lethal with mutations in the genes promoting recovery from stalled replication, such as rqh1, srs2, and mus81, and those involved in nucleotide excision repair like rad13 and rad16. These results suggest that Rad62, like Rad60, in conjunction with the Smc5-6 complex, plays an essential role in maintaining chromosome integrity and recovery from stalled replication by recombination.

* Corresponding author. Mailing address: Department of Molecular Microbiology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan. Phone: 81 6 6879 8317. Fax: 81 6 6879 8320. E-mail: shinagaw{at}biken.osaka-u.ac.jp.

{dagger} Present address: Tsukuba Research Institute, Novartis Pharma, Tsukuba, Ibaraki 300-2611, Japan.

{ddagger} Present address: Graduate School of Integrated Science, Yokohama City University, Tsurumi-ku, Yokohama 230-0045, Japan.

Molecular and Cellular Biology, November 2004, p. 9401-9413, Vol. 24, No. 21
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.21.9401-9413.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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