Journal
NUCLEIC ACIDS RESEARCH
Volume 42, Issue 9, Pages 6038-6051Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku232
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Funding
- MRC [G1100021]
- Wellcome Senior Fellowship [095062]
- The Wellcome Trust [094090]
- BBSRC [BB/E022286/1] Funding Source: UKRI
- MRC [G1100021] Funding Source: UKRI
- Wellcome Trust [095062/Z/10/Z] Funding Source: Wellcome Trust
- 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
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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.
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