Structural highlights
Function[VPS75_YEAST] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.[1] [2] Publication Abstract from PubMedNAP-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. The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.,Bowman A, Hammond CM, Stirling A, Ward R, Shang W, El-Mkami H, Robinson DA, Svergun DI, Norman DG, Owen-Hughes T Nucleic Acids Res. 2014 May;42(9):6038-51. doi: 10.1093/nar/gku232. Epub 2014 Mar, 31. PMID:24688059[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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