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XB-ART-20585
Cell 1994 Nov 04;793:449-58.
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A heterodimeric coiled-coil protein required for mitotic chromosome condensation in vitro.

Hirano T , Mitchison TJ .


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We report here a chromosomal protein that plays an essential role in mitotic chromosome condensation in Xenopus egg extracts. Two polypeptides, designated XCAP-C and XCAP-E, were found to associate with each other in the extracts, presumably forming a heterodimer. During chromosome assembly in mitotic extracts, XCAP-C/E was recruited to the chromatin and formed a discrete internal structure within assembled chromosomes. Antibody blocking experiments showed that XCAP-C function is required for both assembly and structural maintenance of mitotic chromosomes in vitro. Deduced amino acid sequences revealed that the two polypeptides share common structural motifs, consisting of an N-terminal NTP-binding domain, two central coiled-coil regions, and a C-terminal conserved domain. These motifs are highly conserved in a protein family, members of which have been identified recently in both prokaryotes and eukaryotes.

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Species referenced: Xenopus
Genes referenced: smc4
???displayArticle.antibodies??? Smc2 Ab1 Smc2 Ab2 Smc4 Ab1