Investigation of the molecular mechanism of Rtt109 activation by Vps75
The Regulator of Ty1 Transposition protein 106 (Rtt109) is a fungal histone acetyltransferase required for histone H3 K9, K27 and K56 acetylation. These acetylation sites have been linked to processing and folding of nascent H3 and play an integral role in replication- and repair-coupled nucleosome assembly. An intriguing feature of Rtt109 is its activation by two structurally unrelated histone chaperones, Asf1 and Vps75, which likely stimulate Rtt109 activity via different mechanisms. Using an approach combining nuclear magnetic resonance (NMR) spectroscopy, small-angle scattering (SAS) and crystallography we aim to gain an insight into the structural basis for Rtt109 activation and specifity of H3 acetylation. We find that Rtt109 can adopt different structures in solution and that the equilibrium between the two is shifted upon Vps75 association. In addition, we were able to reconstitute a complex containing Rtt109 and both Asf1 and Vps75 and to map the interaction interfaces of this 150 kDa complex. We now intend to further explore the conformational changes of individual subunits in the complex by contrast-variation SANS.
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CARLOMAGNO Teresa; DANILENKO Nataliya; GABEL Frank; GRAZIADEI Andrea and MARTEL Anne. (2016). Investigation of the molecular mechanism of Rtt109 activation by Vps75. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-871
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