Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere.
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- K F Sullivan
- Department of Cell Biology, Scripps Research Institute, La Jolla, California 92037.
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- M Hechenberger
- Department of Cell Biology, Scripps Research Institute, La Jolla, California 92037.
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- K Masri
- Department of Cell Biology, Scripps Research Institute, La Jolla, California 92037.
説明
<jats:p>Centromeres are the differentiated chromosomal domains that specify the mitotic behavior of chromosomes. To examine the molecular basis for the specification of centromeric chromatin, we have cloned a human cDNA that encodes the 17-kD histone-like centromere antigen, CENP-A. Two domains are evident in the 140 aa CENP-A polypeptide: a unique NH2-terminal domain and a 93-amino acid COOH-terminal domain that shares 62% identity with nucleosomal core protein, histone H3. An epitope tagged derivative of CENP-A was faithfully targeted to centromeres when expressed in a variety of animal cells and this targeting activity was shown to reside in the histone-like COOH-terminal domain of CENP-A. These data clearly indicate that the assembly of centromeres is driven, at least in part, by the incorporation of a novel core histone into centromeric chromatin.</jats:p>
収録刊行物
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- The Journal of cell biology
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The Journal of cell biology 127 (3), 581-592, 1994-11-01
Rockefeller University Press