Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast
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چکیده
منابع مشابه
Histone Chaperone Rtt106 Promotes Nucleosome Formation
Background: Rtt106 is a histone H3-H4 chaperone. Results: Rtt106 oligomerizes through its N terminus and binds (H3-H4)2 tetramers in vitro and in vivo. Conclusion: Rtt106 likely deposits (H3-H4)2 tetramers to promote nucleosome assembly. Significance:Determining the stoichiometry ofH3-H4molecules that associate with Rtt106will increase our understanding on how nucleosomes are formed during S ph...
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متن کاملHistone Chaperone-Mediated Nucleosome Assembly Process
A huge amount of information is stored in genomic DNA and this stored information resides inside the nucleus with the aid of chromosomal condensation factors. It has been reported that the repeat nucleosome core particle (NCP) consists of 147-bp of DNA and two copies of H2A, H2B, H3 and H4. Regulation of chromosomal structure is important to many processes inside the cell. In vivo, a group of h...
متن کاملOn the mechanism of nucleosome assembly by histone chaperone NAP1.
The process of mononucleosome assembly mediated by histone chaperone NAP1 was investigated using DNA fragments 146 and 207 bp in length containing the Lytechinus variegatus 5 S rDNA nucleosome positioning sequence. A quantitative description was derived using gel electrophoresis and fluorescent anisotropy data. First, NAP1-bound H3.H4 was released forming a DNA-histone tetramer complex with a t...
متن کاملThe Yeast Histone Chaperone Hif1p Functions with RNA in Nucleosome Assembly
BACKGROUND Hif1p is an H3/H4-specific histone chaperone that associates with the nuclear form of the Hat1p/Hat2p complex (NuB4 complex) in the yeast Saccharomyces cerevisiae. While not capable of depositing histones onto DNA on its own, Hif1p can act in conjunction with a yeast cytosolic extract to assemble nucleosomes onto a relaxed circular plasmid. RESULTS To identify the factor(s) that fu...
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ژورنال
عنوان ژورنال: Nature Communications
سال: 2018
ISSN: 2041-1723
DOI: 10.1038/s41467-017-02759-8