Histones H3 and H4 interact with the ends of nucleosome DNA.
نویسنده
چکیده
Isolated HeLa cell nucleosomes (core particles) were labeled at the 5'-termini of their DNA with 32P using [gamma-32P]ATP and polynucleotide kne by sequential methylation, depurination, Schiff base formation, and reduction with sodium borhydride. After digestion of the noncrosslinked DNA by DNase I and venom phosphodiesterase, histones were separated by gel electrophoresis and those crosslinked to the 5'-termini were identified by 32P-autoradiography. Histones H3 and H4 occur with equeal frequency as the nearest protein neighbors to the end of the DNA in nucleosomes. Histone arrangements within the core particle compatible with these results are discussed.
منابع مشابه
Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork
MCM2 is a subunit of the replicative helicase machinery shown to interact with histones H3 and H4 during the replication process through its N-terminal domain. During replication, this interaction has been proposed to assist disassembly and assembly of nucleosomes on DNA. However, how this interaction participates in crosstalk with histone chaperones at the replication fork remains to be elucid...
متن کاملThe Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation
Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. ...
متن کاملIsolation and characterization of acetylated histones H3 and H4 and their assembly into nucleosomes.
Nucleosome and chromatin structure/function relationships of histone acetylations are not understood. To address these questions we have developed chromatographic procedures that separate subtypes of H3 and the acetylated states of histone H3 and H4 in exceptionally pure forms. The sites of acetylation of the intermediately acetylated states of H3 have been determined and show a specific patter...
متن کاملThe activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4–DNA complexes
The deposition of the histones H3/H4 onto DNA to give the tetrasome intermediate and the displacement of H3/H4 from DNA are thought to be the first and the last steps in nucleosome assembly and disassembly, respectively. Anti-silencing function 1 (Asf1) is a chaperone of the H3/H4 dimer that functions in both of these processes. However, little is known about the thermodynamics of chaperone-his...
متن کاملOpposing roles of H3- and H4-acetylation in the regulation of nucleosome structure—a FRET study
Using FRET in bulk and on single molecules, we assessed the structural role of histone acetylation in nucleosomes reconstituted on the 170 bp long Widom 601 sequence. We followed salt-induced nucleosome disassembly, using donor–acceptor pairs on the ends or in the internal part of the nucleosomal DNA, and on H2B histone for measuring H2A/H2B dimer exchange. This allowed us to distinguish the in...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 73 12 شماره
صفحات -
تاریخ انتشار 1976