期刊
NUCLEIC ACIDS RESEARCH
卷 44, 期 13, 页码 6157-6172出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkw209
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资金
- Wellcome Trust [094090, 097945, 099149]
- Medical Research Council [G1100021]
- Biotechnology and Biological Sciences Research Council [BB/E022286/1] Funding Source: researchfish
- Medical Research Council [G1100021] Funding Source: researchfish
- Wellcome Trust [095062/Z/10/Z] Funding Source: researchfish
- BBSRC [BB/E022286/1] Funding Source: UKRI
- MRC [G1100021] Funding Source: UKRI
- Wellcome Trust [095062/Z/10/Z] Funding Source: Wellcome Trust
Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice. We show Vps75 associates with histones in multiple oligomers. In the presence of equimolar H3-H4 and Vps75, the major species is a reconfigured Vps75 tetramer bound to a histone H3-H4 tetramer. However, in the presence of excess histones, a Vps75 dimer bound to a histone H3-H4 tetramer predominates. We show the Vps75-H3-H4 interaction is compatible with the histone chaperone Asf1 and deduce a structural model of the Vps75-Asf1-H3-H4 (VAH) co-chaperone complex using the Pulsed Electron-electron Double Resonance (PEL-DOR) technique and cross-linking MS/MS distance restraints. The model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer. This provides a structural explanation for many of the complexes detected biochemically and illustrates the ability of Vps75 to interact with dimeric or tetrameric H3-H4 using the same interaction surface.
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