HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-A at centromeres.

By Elaine M. Dunleavy, D. Roche, H. Tagami, N. Lacoste, D. Ray-Gallet, Yusuke Nakamura, Y. Daigo, Y. Nakatani, Geneviève Almouzni-Pettinotti. Cell, 2009

662 citations recorded by the source corpus.

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.

Subfields: Cell Biology, Computer Networks and Communications, Plant Science

View Paper: https://www.semanticscholar.org/paper/3af3308eb3951d2b570d106475d55dfd8c140386

Citations in the corpus

• Centromere-specific assembly of CENP-a nucleosomes is mediated by HJURP. (2009, neutral): “In an accompanying paper, Dunleavy et al. (2009) also demonstrate HJURP to be an essential CENP-A-specific chaperone.”