title: The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.
abstract: NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron-electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a 'self-chaperoning' type mechanism.
authors.affiliation: Centre for Gene Regulation and Expression, University of Dundee, Dundee, DD1 5EH, UK.
authors.forename: Andrew
authors.initials: A
authors.lastname: Bowman
authors.affiliation: Centre for Gene Regulation and Expression, University of Dundee, Dundee, DD1 5EH, UK.
authors.forename: Colin M
authors.initials: CM
authors.lastname: Hammond
authors.affiliation: Centre for Gene Regulation and Expression, University of Dundee, Dundee, DD1 5EH, UK.
authors.forename: Andrew
authors.initials: A
authors.lastname: Stirling
authors.affiliation: Nucleic Acids Structure Research Group, University of Dundee, Dundee, DD1 5EH, UK.
authors.forename: Richard
authors.initials: R
authors.lastname: Ward
authors.affiliation: European Molecular Biology Laboratory, Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Weifeng
authors.initials: W
authors.lastname: Shang
authors.affiliation: School of Physics and Astronomy, University of St Andrews, St Andrews FE2 4KM, UK.
authors.forename: Hassane
authors.initials: H
authors.lastname: El-Mkami
authors.affiliation: Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
authors.forename: David A
authors.initials: DA
authors.lastname: Robinson
authors.affiliation: European Molecular Biology Laboratory, Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Dmitri I
authors.initials: DI
authors.lastname: Svergun
authors.affiliation: Nucleic Acids Structure Research Group, University of Dundee, Dundee, DD1 5EH, UK.
authors.forename: David G
authors.initials: DG
authors.lastname: Norman
authors.affiliation: Centre for Gene Regulation and Expression, University of Dundee, Dundee, DD1 5EH, UK t.a.owenhughes@dundee.ac.uk.
authors.forename: Tom
authors.initials: T
authors.lastname: Owen-Hughes
mesh_terms: D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D056490:Nucleosome Assembly Protein 1 / Q000737:chemistry*; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D053838:Scattering, Small Angle; D012996:Solutions; D014961:X-Ray Diffraction
chemical_list: D018832:Molecular Chaperones; C533556:NAP1 protein, S cerevisiae; D056490:Nucleosome Assembly Protein 1; D029701:Saccharomyces cerevisiae Proteins; D012996:Solutions; C525548:Vps75 protein, S cerevisiae