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-Structure paper
Title | Nucleoplasmin binds histone H2A-H2B dimers through its distal face. |
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Journal, issue, pages | J Biol Chem, Vol. 285, Issue 44, Page 33771-33778, Year 2010 |
Publish date | Oct 29, 2010 |
Authors | Isbaal Ramos / Jaime Martín-Benito / Ron Finn / Laura Bretaña / Kerman Aloria / Jesús M Arizmendi / Juan Ausió / Arturo Muga / José M Valpuesta / Adelina Prado / |
PubMed 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 ...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. |
External links | J Biol Chem / PubMed:20696766 / PubMed Central |
Methods | EM (single particle) |
Resolution | 19.5 - 21.0 Å |
Structure data | EMDB-1777: Structure of the complex Nucleoplamsin:H2A-H2B histones. EMDB-1778: |
Source |
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Keywords | NUCLEAR PROTEIN / CHAPERONE / CHROMATIN / NUCLEAR-CHAPERONE / HISTONE-CHAPERONE |