HJURP interaction with the condensin II complex during G1 promotes CENP-A deposition.
Centromeric chromatin is required for kinetochore assembly during mitosis and accurate chromosome segregation. A unique nucleosome containing the histone H3-specific variant CENP-A is the defining feature of centromeric chromatin. In humans, CENP-A nucleosome deposition occurs in early G1 just after mitotic exit at the time when the CENP-A deposition machinery localizes to centromeres. The mechanism by which CENP-A is deposited onto an existing, condensed chromatin template is not understood. Here we identify the selective association of the CENP-A chaperone HJURP with the condensin II complex and not condensin I. We show CAPH2 is present at centromeres during early G1 at the time when CENP-A deposition is occurring. CAPH2 localization to early G1 centromeres is dependent on HJURP. The CENP-A chaperone and assembly factor HJURP induces decondensation of a noncentromeric LacO array, and this decondensation is modulated by the condensin II complex. We show that condensin II function at the centromere is required for new CENP-A deposition in human cells. These data demonstrate that HJURP selectively recruits the condensin II chromatin-remodeling complex to facilitate CENP-A deposition in human cells.
Department of Biochemistry and Molecular Genetics, University of Virginia Medical School, Charlottesville, VA 22908.
Meghan C
MC
Barnhart-Dailey
Department of Cell Biology, University of Virginia Medical School, Charlottesville, VA 22908.
Prasad
P
Trivedi
Department of Biochemistry and Molecular Genetics, University of Virginia Medical School, Charlottesville, VA 22908.|Department of Cell Biology, University of Virginia Medical School, Charlottesville, VA 22908.
P Todd
PT
Stukenberg
Department of Biochemistry and Molecular Genetics, University of Virginia Medical School, Charlottesville, VA 22908 dfoltz@northwestern.edu.|Department of Cell Biology, University of Virginia Medical School, Charlottesville, VA 22908.|Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611.
Daniel R
DR
Foltz
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001324:Autoantigens / Q000378:metabolism*; D002503:Centromere / Q000378:metabolism*; D000076247:Centromere Protein A; D002843:Chromatin / Q000378:metabolism; D042002:Chromatin Assembly and Disassembly / Q000502:physiology; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D020090:Chromosome Segregation / Q000502:physiology; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D016193:G1 Phase; D006657:Histones / Q000378:metabolism; D006801:Humans; D008938:Mitosis; D046912:Multiprotein Complexes / Q000378:metabolism; D009707:Nucleosomes; D011485:Protein Binding / Q000502:physiology; D012697:Serine Endopeptidases / Q000378:metabolism / Q000502:physiology; D013385:Succinate Dehydrogenase / Q000378:metabolism
D001324:Autoantigens; C000619700:CENPA protein, human; D000076247:Centromere Protein A; D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; C524371:HJURP protein, human; D006657:Histones; D046912:Multiprotein Complexes; D009707:Nucleosomes; C491545:SDHD protein, human; C108312:condensin complexes; D013385:Succinate Dehydrogenase; C472564:PRSS27 protein, human; D012697:Serine Endopeptidases; D000251:Adenosine Triphosphatases