2XQL

Fitting of the H2A-H2B histones in the electron microscopy map of the complex Nucleoplasmin:H2A-H2B histones (1:5).

Summary for 2XQL

• Entry DOI: 10.2210/pdb2xql/pdb
• Related: 1EQZ 1HIO 1HQ3 1TZY 2ARO 2HIO
• EMDB information: 1777
• Descriptor: HISTONE H2A-IV, HISTONE H2B 5 (2 entities in total)
• Functional Keywords: nuclear protein, chaperone, chromatin, nuclear-chaperone, histone-chaperone
• Biological source: GALLUS GALLUS (CHICKEN); More
• Cellular location: Nucleus: P02263 P0C1H4
• Total number of polymer chains: 10
• Total formula weight: 100060.40

Authors

Ramos, I.,Martin-Benito, J.,Finn, R.,Bretana, L.,Aloria, K.,Arizmendi, J.M.,Ausio, J.,Muga, A.,Valpuesta, J.M.,Prado, A. (deposition date: 2010-09-02, release date: 2010-11-03, Last modification date: 2024-05-08)

Primary citation

Ramos, I.,Martin-Benito, J.,Finn, R.,Bretana, L.,Aloria, K.,Arizmendi, J.M.,Ausio, J.,Muga, A.,Valpuesta, J.M.,Prado, A.
Nucleoplasmin Binds Histone H2A-H2B Dimers Through its Distal Face.
J.Biol.Chem., 285:33771-, 2010

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 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.

PubMed: 20696766
DOI: 10.1074/JBC.M110.150664

Experimental method

ELECTRON MICROSCOPY (19.5 Å)