Centromere assembly requires the direct recognition of CENP-A nucleosomes by CENP-N.

Abstract:

:Centromeres are specialized chromosomal domains that direct kinetochore assembly during mitosis. CENP-A (centromere protein A), a histone H3-variant present exclusively in centromeric nucleosomes, is thought to function as an epigenetic mark that specifies centromere identity. Here we identify the essential centromere protein CENP-N as the first protein to selectively bind CENP-A nucleosomes but not H3 nucleosomes. CENP-N bound CENP-A nucleosomes in a DNA sequence-independent manner, but did not bind soluble CENP-A-H4 tetramers. Mutations in CENP-N that reduced its affinity for CENP-A nucleosomes caused defects in CENP-N localization and had dominant effects on the recruitment of CENP-H, CENP-I and CENP-K to centromeres. Depletion of CENP-N using siRNA (short interfering RNA) led to similar centromere assembly defects and resulted in reduced assembly of nascent CENP-A into centromeric chromatin. These data suggest that CENP-N interprets the information encoded within CENP-A nucleosomes and recruits other proteins to centromeric chromatin that are required for centromere function and propagation.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Carroll CW,Silva MC,Godek KM,Jansen LE,Straight AF

doi

10.1038/ncb1899

subject

Has Abstract

pub_date

2009-07-01 00:00:00

pages

896-902

issue

7

eissn

1465-7392

issn

1476-4679

pii

ncb1899

journal_volume

11

pub_type

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