TY - JOUR
T1 - HJURP Is a Cell-Cycle-Dependent Maintenance and Deposition Factor of CENP-A at Centromeres
AU - Dunleavy, Elaine M.
AU - Roche, Danièle
AU - Tagami, Hideaki
AU - Lacoste, Nicolas
AU - Ray-Gallet, Dominique
AU - Nakamura, Yusuke
AU - Daigo, Yataro
AU - Nakatani, Yoshihiro
AU - Almouzni-Pettinotti, Geneviève
PY - 2009/5/1
Y1 - 2009/5/1
N2 - The histone H3 variant CenH3, called CENP-A in humans, is central in centromeric chromatin to ensure proper chromosome segregation. In the absence of an underlying DNA sequence, it is still unclear how CENP-A deposition at centromeres is determined. Here, we purified non-nucleosomal CENP-A complexes to identify direct CENP-A partners involved in such a mechanism and identified HJURP. HJURP was not detected in H3.1- or H3.3-containing complexes, indicating its specificity for CENP-A. HJURP centromeric localization is cell cycle regulated, and its transient appearance at the centromere coincides precisely with the proposed time window for new CENP-A deposition. Furthermore, HJURP downregulation leads to a major reduction in CENP-A at centromeres and impairs deposition of newly synthesized CENP-A, causing mitotic defects. We conclude that HJURP is a key factor for CENP-A deposition and maintenance at centromeres.
AB - The histone H3 variant CenH3, called CENP-A in humans, is central in centromeric chromatin to ensure proper chromosome segregation. In the absence of an underlying DNA sequence, it is still unclear how CENP-A deposition at centromeres is determined. Here, we purified non-nucleosomal CENP-A complexes to identify direct CENP-A partners involved in such a mechanism and identified HJURP. HJURP was not detected in H3.1- or H3.3-containing complexes, indicating its specificity for CENP-A. HJURP centromeric localization is cell cycle regulated, and its transient appearance at the centromere coincides precisely with the proposed time window for new CENP-A deposition. Furthermore, HJURP downregulation leads to a major reduction in CENP-A at centromeres and impairs deposition of newly synthesized CENP-A, causing mitotic defects. We conclude that HJURP is a key factor for CENP-A deposition and maintenance at centromeres.
KW - CELLBIO
KW - CELLCYLE
UR - https://www.scopus.com/pages/publications/65249129208
U2 - 10.1016/j.cell.2009.02.040
DO - 10.1016/j.cell.2009.02.040
M3 - Article
SN - 0092-8674
VL - 137
SP - 485
EP - 497
JO - Cell
JF - Cell
IS - 3
ER -