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Ramos I
,
Martín-Benito J
,
Finn R
,
Bretaña L
,
Aloria K
,
Arizmendi JM
,
Ausió J
,
Muga A
,
Valpuesta JM
,
Prado A
.
???displayArticle.abstract??? Nucleoplasmin (NP) is a pentameric chaperone that regulates the condensation state of chromatin extracting specific basic proteins from sperm chromatin and depositing H2A-H2B histone dimers. It has been proposed that histones could bind to either the lateral or distal face of the pentameric structure. Here, we combine different biochemical and biophysical techniques to show that natural, hyperphosphorylated NP can bind five H2A-H2B dimers and that the amount of bound ligand depends on the overall charge (phosphorylation level) of the chaperone. Three-dimensional reconstruction of NP/H2A-H2B complex carried out by electron microscopy reveals that histones interact with the chaperone distal face. Limited proteolysis and mass spectrometry indicate that the interaction results in protection of the histone fold and most of the H2A and H2B C-terminal tails. This structural information can help to understand the function of NP as a histone chaperone.
Akey,
Histone chaperones and nucleosome assembly.
2003, Pubmed
Akey,
Histone chaperones and nucleosome assembly.
2003,
Pubmed
Arnan,
Interaction of nucleoplasmin with core histones.
2003,
Pubmed
,
Xenbase
Ausio,
Use of selectively trypsinized nucleosome core particles to analyze the role of the histone "tails" in the stabilization of the nucleosome.
1989,
Pubmed
Bañuelos,
Phosphorylation of both nucleoplasmin domains is required for activation of its chromatin decondensation activity.
2007,
Pubmed
,
Xenbase
Bañuelos,
Activation mechanism of the nuclear chaperone nucleoplasmin: role of the core domain.
2003,
Pubmed
,
Xenbase
Böhm,
Proteases as structural probes for chromatin: the domain structure of histones.
1984,
Pubmed
Cairns,
Chromatin remodeling complexes: strength in diversity, precision through specialization.
2005,
Pubmed
Chacón,
Multi-resolution contour-based fitting of macromolecular structures.
2002,
Pubmed
Cotten,
Massive phosphorylation distinguishes Xenopus laevis nucleoplasmin isolated from oocytes or unfertilized eggs.
1986,
Pubmed
,
Xenbase
Dimitrov,
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.
1996,
Pubmed
,
Xenbase
Dimitrov,
Remodeling sperm chromatin in Xenopus laevis egg extracts: the role of core histone phosphorylation and linker histone B4 in chromatin assembly.
1994,
Pubmed
,
Xenbase
Dingwall,
Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals.
1987,
Pubmed
,
Xenbase
Dutta,
The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly.
2001,
Pubmed
Eirín-López,
Long-term evolution and functional diversification in the members of the nucleophosmin/nucleoplasmin family of nuclear chaperones.
2006,
Pubmed
Eitoku,
Histone chaperones: 30 years from isolation to elucidation of the mechanisms of nucleosome assembly and disassembly.
2008,
Pubmed
English,
Structural basis for the histone chaperone activity of Asf1.
2006,
Pubmed
,
Xenbase
Fernández-Sáiz,
Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics.
2006,
Pubmed
Frehlick,
New insights into the nucleophosmin/nucleoplasmin family of nuclear chaperones.
2007,
Pubmed
Hierro,
Electrostatic interactions at the C-terminal domain of nucleoplasmin modulate its chromatin decondensation activity.
2002,
Pubmed
,
Xenbase
Hierro,
Structural and functional properties of Escherichia coli-derived nucleoplasmin. A comparative study of recombinant and natural proteins.
2001,
Pubmed
,
Xenbase
Karantza,
Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimer stability.
1995,
Pubmed
Lee,
Crystal structure of human nucleophosmin-core reveals plasticity of the pentamer-pentamer interface.
2007,
Pubmed
Ludtke,
EMAN: semiautomated software for high-resolution single-particle reconstructions.
1999,
Pubmed
Luger,
Crystal structure of the nucleosome core particle at 2.8 A resolution.
1997,
Pubmed
Mazurkiewicz,
On the mechanism of nucleosome assembly by histone chaperone NAP1.
2006,
Pubmed
Muto,
Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity.
2007,
Pubmed
Namboodiri,
The structure and function of Xenopus NO38-core, a histone chaperone in the nucleolus.
2004,
Pubmed
,
Xenbase
Namboodiri,
The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding.
2003,
Pubmed
Park,
Histone chaperones in nucleosome eviction and histone exchange.
2008,
Pubmed
Prado,
Nucleoplasmin: a nuclear chaperone.
2004,
Pubmed
,
Xenbase
Prieto,
Nucleoplasmin interaction with protamines. Involvement of the polyglutamic tract.
2002,
Pubmed
,
Xenbase
Ramos,
Nucleoplasmin-mediated unfolding of chromatin involves the displacement of linker-associated chromatin proteins.
2005,
Pubmed
,
Xenbase
Salvany,
Mutation of the small acidic tract A1 drastically reduces nucleoplasmin activity.
2004,
Pubmed
,
Xenbase
Shevchenko,
Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels.
1996,
Pubmed
Sorzano,
XMIPP: a new generation of an open-source image processing package for electron microscopy.
2004,
Pubmed
Taneva,
A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models.
2009,
Pubmed
,
Xenbase
Taneva,
Activation of nucleoplasmin, an oligomeric histone chaperone, challenges its stability.
2008,
Pubmed
Zhou,
NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B.
2008,
Pubmed
