Abstract:
:The rad18 gene of Schizosaccharomyces pombe is an essential gene that is involved in several different DNA repair processes. Rad18 (Smc6) is a member of the structural maintenance of chromosomes (SMC) family and, together with its SMC partner Spr18 (Smc5), forms the core of a high-molecular-weight complex. We show here that both S. pombe and human Smc5 and -6 interact through their hinge domains and that four independent temperature-sensitive mutants of Rad18 (Smc6) are all mutated at the same glycine residue in the hinge region. This mutation abolishes the interactions between the hinge regions of Rad18 (Smc6) and Spr18 (Smc5), as does mutation of a conserved glycine in the hinge region of Spr18 (Smc5). We purified the Smc5-6 complex from S. pombe and identified four non-SMC components, Nse1, Nse2, Nse3, and Rad62. Nse3 is a novel protein which is related to the mammalian MAGE protein family, many members of which are specifically expressed in cancer tissue. In initial steps to understand the architecture of the complex, we identified two subcomplexes containing Rad18-Spr18-Nse2 and Nse1-Nse3-Rad62. The subcomplexes are probably bridged by a weaker interaction between Nse2 and Nse3.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Sergeant J,Taylor E,Palecek J,Fousteri M,Andrews EA,Sweeney S,Shinagawa H,Watts FZ,Lehmann ARdoi
10.1128/MCB.25.1.172-184.2005subject
Has Abstractpub_date
2005-01-01 00:00:00pages
172-84issue
1eissn
0270-7306issn
1098-5549pii
25/1/172journal_volume
25pub_type
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