scholarly journals The Chromatin Assembly Factor 1 Promotes Rad51-Dependent Template Switches at Replication Forks by Counteracting D-Loop Disassembly by the RecQ-Type Helicase Rqh1

PLoS Biology ◽  
2014 ◽  
Vol 12 (10) ◽  
pp. e1001968 ◽  
Author(s):  
Violena Pietrobon ◽  
Karine Fréon ◽  
Julien Hardy ◽  
Audrey Costes ◽  
Ismail Iraqui ◽  
...  
Keyword(s):  
Chromatin Assembly ◽  
Replication Forks ◽  
Chromatin Assembly Factor ◽  
Assembly Factor ◽  
D Loop ◽  
Template Switches

scholarly journals Two Fundamentally Distinct PCNA Interaction Peptides Contribute to Chromatin Assembly Factor 1 Function

2009 ◽  
Vol 29 (24) ◽  
pp. 6353-6365 ◽  
Author(s):  
Tom Rolef Ben-Shahar ◽  
Araceli G. Castillo ◽  
Michael J. Osborne ◽  
Katherine L. B. Borden ◽  
Jack Kornblatt ◽  
...  
Keyword(s):  
Dna Replication ◽  
Large Subunit ◽  
Chromatin Assembly ◽  
Nuclear Antigen ◽  
Replication Forks ◽  
Nucleosome Assembly ◽  
Chromatin Assembly Factor ◽  
Assembly Factor

ABSTRACT Chromatin assembly factor 1 (CAF-1) deposits histones H3 and H4 rapidly behind replication forks through an interaction with the proliferating cell nuclear antigen (PCNA), a DNA polymerase processivity factor that also binds to a number of replication enzymes and other proteins that act on nascent DNA. The mechanisms that enable CAF-1 and other PCNA-binding proteins to function harmoniously at the replication fork are poorly understood. Here we report that the large subunit of human CAF-1 (p150) contains two distinct PCNA interaction peptides (PIPs). The N-terminal PIP binds strongly to PCNA in vitro but, surprisingly, is dispensable for nucleosome assembly and only makes a modest contribution to targeting p150 to DNA replication foci in vivo. In contrast, the internal PIP (PIP2) lacks one of the highly conserved residues of canonical PIPs and binds weakly to PCNA. Surprisingly, PIP2 is essential for nucleosome assembly during DNA replication in vitro and plays a major role in targeting p150 to sites of DNA replication. Unlike canonical PIPs, such as that of p21, the two p150 PIPs are capable of preferentially inhibiting nucleosome assembly, rather than DNA synthesis, suggesting that intrinsic features of these peptides are part of the mechanism that enables CAF-1 to function behind replication forks without interfering with other PCNA-mediated processes.

scholarly journals A separable domain of the p150 subunit of human chromatin assembly factor-1 promotes protein and chromosome associations with nucleoli

2014 ◽  
Vol 25 (18) ◽  
pp. 2866-2881 ◽  
Author(s):  
Corey L. Smith ◽  
Timothy D. Matheson ◽  
Daniel J. Trombly ◽  
Xiaoming Sun ◽  
Eric Campeau ◽  
...  
Keyword(s):  
Repetitive Element ◽  
Chromatin Assembly ◽  
The Other ◽  
Dna Interactions ◽  
Interaction Sites ◽  
Chromatin Assembly Factor ◽  
Nucleolar Proteins ◽  
Nucleolar Chromosome ◽  
Assembly Factor ◽  
Chromosome Associations

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.

scholarly journals Essential Role of Chromatin Assembly Factor-1–mediated Rapid Nucleosome Assembly for DNA Replication and Cell Division in Vertebrate Cells

2007 ◽  
Vol 18 (1) ◽  
pp. 129-141 ◽  
Author(s):  
Yasunari Takami ◽  
Tatsuya Ono ◽  
Tatsuo Fukagawa ◽  
Kei-ichi Shibahara ◽  
Tatsuo Nakayama
Keyword(s):  
Dna Replication ◽  
Essential Role ◽  
Chromatin Assembly ◽  
Nuclear Antigen ◽  
Nucleosome Assembly ◽  
Chromatin Assembly Factor ◽  
Assembly Factor

Chromatin assembly factor-1 (CAF-1), a complex consisting of p150, p60, and p48 subunits, is highly conserved from yeast to humans and facilitates nucleosome assembly of newly replicated DNA in vitro. To investigate roles of CAF-1 in vertebrates, we generated two conditional DT40 mutants, respectively, devoid of CAF-1p150 and p60. Depletion of each of these CAF-1 subunits led to delayed S-phase progression concomitant with slow DNA synthesis, followed by accumulation in late S/G2 phase and aberrant mitosis associated with extra centrosomes, and then the final consequence was cell death. We demonstrated that CAF-1 is necessary for rapid nucleosome formation during DNA replication in vivo as well as in vitro. Loss of CAF-1 was not associated with the apparent induction of phosphorylations of S-checkpoint kinases Chk1 and Chk2. To elucidate the precise role of domain(s) in CAF-1p150, functional dissection analyses including rescue assays were preformed. Results showed that the binding abilities of CAF-1p150 with CAF-1p60 and DNA polymerase sliding clamp proliferating cell nuclear antigen (PCNA) but not with heterochromatin protein HP1-γ are required for cell viability. These observations highlighted the essential role of CAF-1–dependent nucleosome assembly in DNA replication and cell proliferation through its interaction with PCNA.

Chromatin Assembly Factor-1/p60 overexpression: a potential index of psoriasis severity

2014 ◽  
Vol 24 (4) ◽  
pp. 509-511 ◽  
Author(s):  
Massimo Mascolo ◽  
Fabio Ayala ◽  
Gennaro Ilardi ◽  
Anna Balato ◽  
Serena Lembo
Keyword(s):  
Chromatin Assembly ◽  
Chromatin Assembly Factor ◽  
Potential Index ◽  
Assembly Factor ◽  
Psoriasis Severity

scholarly journals Chromatin Assembly Factor 1 (CAF-1) facilitates the establishment of facultative heterochromatin during pluripotency exit

2019 ◽  
Vol 47 (21) ◽  
pp. 11114-11131 ◽  
Author(s):  
Liang Cheng ◽  
Xu Zhang ◽  
Yan Wang ◽  
Haiyun Gan ◽  
Xiaowei Xu ◽  
...  
Keyword(s):  
Cell Fate ◽  
Embryonic Stem ◽  
Chromatin Assembly ◽  
Nuclear Antigen ◽  
Gene Promoters ◽  
Cell Fate Determination ◽  
Nucleosome Assembly ◽  
Fate Determination ◽  
Chromatin Assembly Factor ◽  
Assembly Factor

Abstract Establishment and subsequent maintenance of distinct chromatin domains during embryonic stem cell (ESC) differentiation are crucial for lineage specification and cell fate determination. Here we show that the histone chaperone Chromatin Assembly Factor 1 (CAF-1), which is recruited to DNA replication forks through its interaction with proliferating cell nuclear antigen (PCNA) for nucleosome assembly, participates in the establishment of H3K27me3-mediated silencing during differentiation. Deletion of CAF-1 p150 subunit impairs the silencing of many genes including Oct4, Sox2 and Nanog as well as the establishment of H3K27me3 at these gene promoters during ESC differentiation. Mutations of PCNA residues involved in recruiting CAF-1 to the chromatin also result in defects in differentiation in vitro and impair early embryonic development as p150 deletion. Together, these results reveal that the CAF-1-PCNA nucleosome assembly pathway plays an important role in the establishment of H3K27me3-mediated silencing during cell fate determination.

scholarly journals Control of trichome branching by Chromatin Assembly Factor-1

2008 ◽  
Vol 8 (1) ◽  
pp. 54 ◽  
Author(s):  
Vivien Exner ◽  
Wilhelm Gruissem ◽  
Lars Hennig
Keyword(s):  
Chromatin Assembly ◽  
Chromatin Assembly Factor ◽  
Assembly Factor
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