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Vol. 12, Issue 6, 1583-1594, June 2001
and
*MRC Cell Mutation Unit, University of Sussex, Falmer, Brighton BN1
9RR, United Kingdom, 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 and
spr18 and designated them hSMC6 and
hSMC5. 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.
Department of Cell Biology and
Genetics, Erasmus University, Rotterdam, The Netherlands and
Department of Biology, York University, Downsview,
Ontario M3J 1P3, Canada
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