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.
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Citation: 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
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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