DOI: 10.1091/mbc.12.6.1583. Characterization of a Novel Human SMC Heterodimer Homologous to the<i>Schizosaccharomyces pombe</i>Rad18/Spr18 Complex

Characterization of a Novel Human SMC Heterodimer Homologous to theSchizosaccharomyces pombeRad18/Spr18 Complex

10.1091/mbc.12.6.1583

Crossref journal-article

American Society for Cell Biology (ASCB)

Molecular Biology of the Cell (1076)

Abstract

The structural maintenance of chromosomes (SMC) protein encoded by the fission yeast rad18 gene is involved in several DNA repair processes and has an essential function in DNA replication and mitotic control. It has a heterodimeric partner SMC protein, Spr18, with which it forms the core of a multiprotein complex. We have now isolated the human orthologues of rad18 andspr18 and designated them hSMC6 andhSMC5. Both proteins are about 1100 amino acids in length and are 27–28% identical to their fission yeast orthologues, with much greater identity within their N- and C-terminal globular domains. The hSMC6 and hSMC5 proteins interact to form a tight complex analogous to the yeast Rad18/Spr18 heterodimer. In proliferating human cells the proteins are bound to both chromatin and the nucleoskeleton. In addition, we have detected a phosphorylated form of hSMC6 that localizes to interchromatin granule clusters. Both the total level of hSMC6 and its phosphorylated form remain constant through the cell cycle. Both hSMC5 and hSMC6 proteins are expressed at extremely high levels in the testis and associate with the sex chromosomes in the late stages of meiotic prophase, suggesting a possible role for these proteins in meiosis.

Bibliography

Taylor, E. M., Moghraby, J. S., Lees, J. H., Smit, B., Moens, P. B., & Lehmann, A. R. (2001). Characterization of a Novel Human SMC Heterodimer Homologous to theSchizosaccharomyces pombeRad18/Spr18 Complex. Molecular Biology of the Cell, 12(6), 1583â1594.

Authors 6

Elaine M. Taylor (first)
Jeelan S. Moghraby (additional)
Jennifer H. Lees (additional)
Bep Smit (additional)
Peter B. Moens (additional)
Alan R. Lehmann (additional)

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Dates

Type	When
Created	12 years, 1 month ago (July 2, 2013, 8:15 p.m.)
Deposited	3 years, 6 months ago (Feb. 26, 2022, 9:45 p.m.)
Indexed	3 weeks, 4 days ago (Aug. 7, 2025, 4:47 p.m.)
Issued	24 years, 3 months ago (June 1, 2001)
Published	24 years, 3 months ago (June 1, 2001)
Published Print	24 years, 3 months ago (June 1, 2001)

Funders 0

None

BibTeX

@article{Taylor_2001, title={Characterization of a Novel Human SMC Heterodimer Homologous to theSchizosaccharomyces pombeRad18/Spr18 Complex}, volume={12}, ISSN={1939-4586}, url={http://dx.doi.org/10.1091/mbc.12.6.1583}, DOI={10.1091/mbc.12.6.1583}, number={6}, journal={Molecular Biology of the Cell}, publisher={American Society for Cell Biology (ASCB)}, author={Taylor, Elaine M. and Moghraby, Jeelan S. and Lees, Jennifer H. and Smit, Bep and Moens, Peter B. and Lehmann, Alan R.}, editor={Blackburn, Elizabeth H.}, year={2001}, month=jun, pages={1583–1594} }

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  "abstract": "<jats:p>The structural maintenance of chromosomes (SMC) protein encoded by the fission yeast rad18 gene is involved in several DNA repair processes and has an essential function in DNA replication and mitotic control. It has a heterodimeric partner SMC protein, Spr18, with which it forms the core of a multiprotein complex. We have now isolated the human orthologues of rad18 andspr18 and designated them hSMC6 andhSMC5. Both proteins are about 1100 amino acids in length and are 27\u201328% identical to their fission yeast orthologues, with much greater identity within their N- and C-terminal globular domains. The hSMC6 and hSMC5 proteins interact to form a tight complex analogous to the yeast Rad18/Spr18 heterodimer. In proliferating human cells the proteins are bound to both chromatin and the nucleoskeleton. In addition, we have detected a phosphorylated form of hSMC6 that localizes to interchromatin granule clusters. Both the total level of hSMC6 and its phosphorylated form remain constant through the cell cycle. Both hSMC5 and hSMC6 proteins are expressed at extremely high levels in the testis and associate with the sex chromosomes in the late stages of meiotic prophase, suggesting a possible role for these proteins in meiosis.</jats:p>",
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