Nucleosome thermodynamics, histone modifications, and histone chaperone function
نویسندگان
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...
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 کاملP-98: Effect of Mouse Embryo Vitrification on Histone Modifications
Background: Vitrification has been usually used as an assisted reproductive technology in animals and humans. This method needs high concentrations of cryoprotectants that can be toxic with high cooling degrees. Then, vitrification could be change histone modifications such as methylation and acetylation can performance as regulatory controls of gene transcription. So, the purpose of the presen...
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 histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions.
The organization of the eukaryotic genome into nucleosomes dramatically affects the regulation of gene expression. The delicate balance between transcription and DNA compaction relies heavily on nucleosome dynamics. Surprisingly, little is known about the free energy required to assemble these large macromolecular complexes and maintain them under physiological conditions. Here, we describe the...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2010
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.24.1_supplement.310.2