The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones

The role of Nucleoplasmin (NP) as a H2A-H2B histone chaperone has been extensively characterized. To understand its putative interaction with other histone ligands, we have characterized its ability to bind H3-H4 and histone octamers. We find that the chaperone forms distinct complexes with histones...

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Bibliographic Details
Published in:Nucleic acids research 2014-01, Vol.42 (2), p.1311-1325
Main Authors: Ramos, Isbaal, Fernández-Rivero, Noelia, Arranz, Rocío, Aloria, Kerman, Finn, Ron, Arizmendi, Jesús M, Ausió, Juan, Valpuesta, José María, Muga, Arturo, Prado, Adelina
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Histones - chemistry
Histones - metabolism
Intrinsically Disordered Proteins - chemistry
Intrinsically Disordered Proteins - metabolism
Molecular Sequence Data
Nucleoplasmins - chemistry
Nucleoplasmins - metabolism
Protein Multimerization
Proteolysis
Structural Biology
Xenopus laevis
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Summary:The role of Nucleoplasmin (NP) as a H2A-H2B histone chaperone has been extensively characterized. To understand its putative interaction with other histone ligands, we have characterized its ability to bind H3-H4 and histone octamers. We find that the chaperone forms distinct complexes with histones, which differ in the number of molecules that build the assembly and in their spatial distribution. When complexed with H3-H4 tetramers or histone octamers, two NP pentamers form an ellipsoidal particle with the histones located at the center of the assembly, in stark contrast with the NP/H2A-H2B complex that contains up to five histone dimers bound to one chaperone pentamer. This particular assembly relies on the ability of H3-H4 to form tetramers either in solution or as part of the octamer, and it is not observed when a variant of H3 (H3C110E), unable to form stable tetramers, is used instead of the wild-type protein. Our data also suggest that the distal face of the chaperone is involved in the interaction with distinct types of histones, as supported by electron microscopy analysis of the different NP/histone complexes. The use of the same structural region to accommodate all type of histones could favor histone exchange and nucleosome dynamics.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkt899