title: A separable domain of the p150 subunit of human chromatin assembly factor-1 promotes protein and chromosome associations with nucleoli.
abstract: Chromatin assembly factor-1 (CAF-1) is a three-subunit protein complex conserved throughout eukaryotes that deposits histones during DNA synthesis. Here we present a novel role for the human p150 subunit in regulating nucleolar macromolecular interactions. Acute depletion of p150 causes redistribution of multiple nucleolar proteins and reduces nucleolar association with several repetitive element-containing loci. Of note, a point mutation in a SUMO-interacting motif (SIM) within p150 abolishes nucleolar associations, whereas PCNA or HP1 interaction sites within p150 are not required for these interactions. In addition, acute depletion of SUMO-2 or the SUMO E2 ligase Ubc9 reduces α-satellite DNA association with nucleoli. The nucleolar functions of p150 are separable from its interactions with the other subunits of the CAF-1 complex because an N-terminal fragment of p150 (p150N) that cannot interact with other CAF-1 subunits is sufficient for maintaining nucleolar chromosome and protein associations. Therefore these data define novel functions for a separable domain of the p150 protein, regulating protein and DNA interactions at the nucleolus.
authors: Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605.
authors: Corey L
authors: CL
authors: Smith
authors: Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605.
authors: Timothy D
authors: TD
authors: Matheson
authors: Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605.
authors: Daniel J
authors: DJ
authors: Trombly
authors: Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605.
authors: Xiaoming
authors: X
authors: Sun
authors: Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605.
authors: Eric
authors: E
authors: Campeau
authors: Department of Chemical Physiology, Scripps Research Institute, La Jolla, CA 92037.
authors: Xuemei
authors: X
authors: Han
authors: Department of Chemical Physiology, Scripps Research Institute, La Jolla, CA 92037.
authors: John R
authors: JR
authors: Yates
authors: Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605 paul.kaufman1@umassmed.edu.
authors: Paul D
authors: PD
authors: Kaufman
mesh_terms: D002466:Cell Nucleolus / Q000378:metabolism*; D056504:Chromatin Assembly Factor-1 / Q000502:physiology*; D002877:Chromosomes, Human / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D019394:Ki-67 Antigen / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D021381:Protein Transport; D014157:Transcription Factors
chemical_list: C489780:CNOT8 protein, human; D056504:Chromatin Assembly Factor-1; D019394:Ki-67 Antigen; D014157:Transcription Factors