Program in Gene Function and Expression; Program in Molecular Medicine
Biochemistry | Cell Biology | Genetics and Genomics | Molecular Biology | Molecular Genetics
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. Notably, 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. Additionally, acute depletion of SUMO-2 or the SUMO E2 ligase Ubc9 reduces alpha-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.
DOI of Published Version
Smith CL, Matheson TD, Trombly DJ, Sun X, Campeau E, Han X, Yates JR 3rd, Kaufman PD. A separable domain of the p150 subunit of human Chromatin Assembly Factor-1 promotes protein and chromosome associations with nucleoli. Mol Biol Cell. 2014 Sep 15;25(18):2866-81. doi: 10.1091/mbc.E14-05-1029. Epub 2014 Jul 23. Link to article on publisher's site
Molecular biology of the cell
Smith, Corey L.; Matheson, Timothy D.; Trombly, Daniel J.; Sun, Xiaoming; Campeau, Eric; Han, Xuemei; Yates, John R. III; and Kaufman, Paul D., "A separable domain of the p150 subunit of human Chromatin Assembly Factor-1 promotes protein and chromosome associations with nucleoli" (2014). Program in Gene Function and Expression Publications and Presentations. 254.
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