Association states of nucleosome assembly protein 1 and its complexes with histones
- PMID: 15687486
- DOI: 10.1074/jbc.M413329200
Association states of nucleosome assembly protein 1 and its complexes with histones
Abstract
The histone chaperone NAP1 is a carrier of histones during nuclear import, nucleosome assembly, and chromatin remodeling. Analytical ultracentrifugation was used to determine the association states of NAP1 alone and in complexes with core histones. In addition, the concentration dependence of the association was quantified by determining the equilibrium dissociation constant between different NAP1 species. At physiological protein and salt concentrations the prevalent species were the NAP1 dimer and octamer. These were also the association states found to interact with histones in a stoichiometry of one NAP1 monomer per histone. Based on these results a model for a cell cycle-dependent shift of the NAP1 dimer-octamer equilibrium is proposed that reflects different biological functions of NAP1.
Similar articles
-
Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly.EMBO J. 2016 Jul 1;35(13):1465-82. doi: 10.15252/embj.201694105. Epub 2016 May 25. EMBO J. 2016. PMID: 27225933 Free PMC article.
-
Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino-terminal histone tails.J Biol Chem. 2003 Nov 7;278(45):44574-83. doi: 10.1074/jbc.M305636200. Epub 2003 Aug 19. J Biol Chem. 2003. PMID: 12928440
-
Assembly, remodeling, and histone binding capabilities of yeast nucleosome assembly protein 1.J Biol Chem. 1998 Mar 13;273(11):6582-90. doi: 10.1074/jbc.273.11.6582. J Biol Chem. 1998. PMID: 9497395
-
[Physiological functions of the acidic molecular chaperone Nap1].Seikagaku. 2005 Mar;77(3):206-12. Seikagaku. 2005. PMID: 15835307 Review. Japanese. No abstract available.
-
Chromatin assembly: biochemical identities and genetic redundancy.Curr Opin Genet Dev. 1999 Apr;9(2):185-90. doi: 10.1016/S0959-437X(99)80028-8. Curr Opin Genet Dev. 1999. PMID: 10322140 Review.
Cited by
-
Single-molecule FRET method to investigate the dynamics of transcription elongation through the nucleosome by RNA polymerase II.Methods. 2019 Apr 15;159-160:51-58. doi: 10.1016/j.ymeth.2019.01.009. Epub 2019 Jan 17. Methods. 2019. PMID: 30660864 Free PMC article.
-
The structure of nucleosome assembly protein 1.Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1248-53. doi: 10.1073/pnas.0508002103. Epub 2006 Jan 23. Proc Natl Acad Sci U S A. 2006. PMID: 16432217 Free PMC article.
-
The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.Nucleic Acids Res. 2014 May;42(9):6038-51. doi: 10.1093/nar/gku232. Epub 2014 Mar 31. Nucleic Acids Res. 2014. PMID: 24688059 Free PMC article.
-
Nucleosome Dynamics during Transcription Elongation.ACS Chem Biol. 2020 Dec 18;15(12):3133-3142. doi: 10.1021/acschembio.0c00617. Epub 2020 Dec 2. ACS Chem Biol. 2020. PMID: 33263994 Free PMC article.
-
The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation.Mol Cell. 2011 Feb 18;41(4):398-408. doi: 10.1016/j.molcel.2011.01.025. Mol Cell. 2011. PMID: 21329878 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials
