Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Autoantigens / chemistry
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Base Sequence
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Cattle
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Centromere / metabolism*
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Centromere Protein A
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Chromosomal Proteins, Non-Histone / biosynthesis
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Chromosomal Proteins, Non-Histone / chemistry*
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Chromosomal Proteins, Non-Histone / metabolism
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Cloning, Molecular
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Fluorescent Antibody Technique
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HeLa Cells
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Histones / chemistry*
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Histones / metabolism
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Humans
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Immunoblotting
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Molecular Sequence Data
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Muntjacs
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Oligodeoxyribonucleotides
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Protein Folding*
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Recombinant Fusion Proteins / chemistry
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Sequence Homology, Amino Acid
Substances
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Autoantigens
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CENPA protein, human
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Centromere Protein A
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Chromosomal Proteins, Non-Histone
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Histones
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Oligodeoxyribonucleotides
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Recombinant Fusion Proteins
Associated data
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GENBANK/U14518
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GENBANK/U14519