A Conserved Mechanism for Centromeric Nucleosome Recognition by Centromere Protein CENP-C
Copyright policy )A Conserved Mechanism for Centromeric Nucleosome Recognition by Centromere Protein CENP-C
Kinetochore Targeting Chromosomes must be segregated accurately during cell division. This is facilitated by the attachment of mitotic spindle microtubules to the kinetochore at the chromosomal centromere. The centromere is marked with the histone H3 variant CenH3 (CENP-A in human), and CENP-C forms part of the inner kinetochore. Kato et al. (p. 1110 ) used structural biology, biochemistry, and mutagenesis to show that CENP-C recognizes CENP-A chromatin via several different interactions. The CENP-C "central domain" makes close contact with the acidic patch of histones H2A/H2B, and the highly conserved "CENP-C motif" senses both the acidic patch and recognizes the hydrophobicity of the otherwise nonconserved CenH3 tail, supporting a conserved mechanism of centromere targeting by the kinetochore.
- National Institute of Health Pakistan
- National Institute of Allergy and Infectious Diseases United States
- National Institutes of Health United States
- National Institute of Diabetes and Digestive and Kidney Diseases United States
- Stanford University United States
Binding Sites, Chromosomal Proteins, Non-Histone, Amino Acid Motifs, Centromere, Molecular Sequence Data, Autoantigens, Protein Structure, Secondary, Nucleosomes, Histones, Animals, Humans, Drosophila, Amino Acid Sequence, Hydrophobic and Hydrophilic Interactions, Centromere Protein A, Conserved Sequence
Binding Sites, Chromosomal Proteins, Non-Histone, Amino Acid Motifs, Centromere, Molecular Sequence Data, Autoantigens, Protein Structure, Secondary, Nucleosomes, Histones, Animals, Humans, Drosophila, Amino Acid Sequence, Hydrophobic and Hydrophilic Interactions, Centromere Protein A, Conserved Sequence
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