25-30 August 2019
Henry Ford Building
Europe/Berlin timezone

High molecular-weight complexes in the regulation of gene expression: a view by integrative structural biology

28 Aug 2019, 11:55
Max Kade Auditorium (Henry Ford Building)

Max Kade Auditorium

Henry Ford Building

Invited talk Biological applications Biomolecules


Prof. Teresa Carlomagno (Leibniz Universität Hannover)


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. Rtt109 is unique in its activation, performed by two structurally unrelated histone chaperones, Asf1 and Vps75. These proteins stimulate Rtt109 activity via different mechanisms. Rtt109 - Asf1 association has been proposed to be responsible for K56 acetylation, while the Rtt109-Vps75 interaction is required for K9 acetylation.

In our work we find that Rtt109, Vps75 and Asf1 are capable of assembling as a previously uncharacterized complex onto the substrate H3-H4 dimer. Using an integrative structural biology approach based on a powerful combination of solution state NMR and small angle neutron scattering (SANS) we solve the structure of this complex and provide a structural basis for the efficiency and selectivity of acetylation at the at the H3 K9, K27 and K56 sites.

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