Nucleoplasmin binds histone H2A-H2B dimers through its distal face.
作者： Isbaal Ramos , Jaime Martín-Benito , Ron Finn , Laura Bretaña , Kerman Aloria
关键词:
摘要: Nucleoplasmin (NP) is a pentameric chaperone that regulates the condensation state of chromatin extracting specific basic proteins from sperm and depositing H2A-H2B histone dimers. It has been proposed histones could bind to either lateral or distal face structure. Here, we combine different biochemical biophysical techniques show natural, hyperphosphorylated NP can five dimers amount bound ligand depends on overall charge (phosphorylation level) chaperone. Three-dimensional reconstruction NP/H2A-H2B complex carried out by electron microscopy reveals interact with face. Limited proteolysis mass spectrometry indicate interaction results in protection fold most H2A H2B C-terminal tails. This structural information help understand function as
rcsb.org参考文章(41)
S. Dimitrov, A. P. Wolffe, Remodeling somatic nuclei in Xenopus laevis egg extracts: molecular mechanisms for the selective release of histones H1 and H1(0) from chromatin and the acquisition of transcriptional competence. The EMBO Journal. ,vol. 15, pp. 5897- 5906 ,(1996) , 10.1002/J.1460-2075.1996.TB00976.X
Richard J Simpson, Richard J Simpson, Proteins and proteomics : a laboratory manual Cold Spring Harbor Laboratory Press. ,(2003)
C. Dingwall, S.M. Dilworth, S.J. Black, S.E. Kearsey, L.S. Cox, R.A. Laskey, Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals. The EMBO Journal. ,vol. 6, pp. 69- 74 ,(1987) , 10.1002/J.1460-2075.1987.TB04720.X
Joachim Frank, Three-Dimensional Electron Microscopy of Macromolecular Assemblies Oxford University Press. ,(2006) , 10.1093/ACPROF:OSO/9780195182187.001.0001
Shuchismita Dutta, Ildikó V. Akey, Colin Dingwall, Kari L. Hartman, Tom Laue, Robert T. Nolte, James F. Head, Christopher W. Akey, The Crystal Structure of Nucleoplasmin-Core: Implications for Histone Binding and Nucleosome Assembly Molecular Cell. ,vol. 8, pp. 841- 853 ,(2001) , 10.1016/S1097-2765(01)00354-9
José M. Eirín-López, Lindsay J. Frehlick, Juan Ausió, Long-Term Evolution and Functional Diversification in the Members of the Nucleophosmin/Nucleoplasmin Family of Nuclear Chaperones Genetics. ,vol. 173, pp. 1835- 1850 ,(2006) , 10.1534/GENETICS.106.058990
Juan Ausio, Feng Dong, K.E. van Holde, Use of selectively trypsinized nucleosome core particles to analyze the role of the histone “tails” in the stabilization of the nucleosome Journal of Molecular Biology. ,vol. 206, pp. 451- 463 ,(1989) , 10.1016/0022-2836(89)90493-2
Bradley R Cairns, Chromatin remodeling complexes: strength in diversity, precision through specialization. Current Opinion in Genetics & Development. ,vol. 15, pp. 185- 190 ,(2005) , 10.1016/J.GDE.2005.01.003
Lara Salvany, Manel Chiva, Carme Arnan, Juan Ausió, Juan A. Subirana, Núria Saperas, Mutation of the small acidic tract A1 drastically reduces nucleoplasmin activity. FEBS Letters. ,vol. 576, pp. 353- 357 ,(2004) , 10.1016/J.FEBSLET.2004.07.095
Aitor Hierro, Jesús M. Arizmendi, Sonia Bañuelos, Adelina Prado, Arturo Muga, Electrostatic interactions at the C-terminal domain of nucleoplasmin modulate its chromatin decondensation activity. Biochemistry. ,vol. 41, pp. 6408- 6413 ,(2002) , 10.1021/BI020002R