3Q33

Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation

Summary for 3Q33

• Entry DOI: 10.2210/pdb3q33/pdb
• Related: 3D35 3DM7 3Q35
• Descriptor: Histone acetyltransferase RTT109, Vacuolar protein sorting-associated protein 75, HISTONE H3, ... (6 entities in total)
• Functional Keywords: rtt109:vps75=2:2 stoichiometry complex, histone acetyltransferase, with acetyl coenzyme a (acoa) bound, autoacetylation on rtt109 lys290, nuclear, transferase-chaperone-transcription regulator complex, transferase-chaperone complex, transferase, chaperone-gene regulation complex, chaperone/gene regulation
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Cellular location: Nucleus: Q07794 P53853 P61830
• Total number of polymer chains: 3
• Total formula weight: 80005.95

Authors

Tang, Y.,Yuan, H.,Meeth, K.,Marmorstein, R. (deposition date: 2010-12-21, release date: 2011-02-02, Last modification date: 2024-11-06)

Primary citation

Tang, Y.,Holbert, M.A.,Delgoshaie, N.,Wurtele, H.,Guillemette, B.,Meeth, K.,Yuan, H.,Drogaris, P.,Lee, E.H.,Durette, C.,Thibault, P.,Verreault, A.,Cole, P.A.,Marmorstein, R.
Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation.
Structure, 19:221-231, 2011

PubMed Abstract: Yeast Rtt109 promotes nucleosome assembly and genome stability by acetylating K9, K27, and K56 of histone H3 through interaction with either of two distinct histone chaperones, Vps75 or Asf1. We report the crystal structure of an Rtt109-AcCoA/Vps75 complex revealing an elongated Vps75 homodimer bound to two globular Rtt109 molecules to form a symmetrical holoenzyme with a ∼12 Å diameter central hole. Vps75 and Rtt109 residues that mediate complex formation in the crystals are also important for Rtt109-Vps75 interaction and H3K9/K27 acetylation both in vitro and in yeast cells. The same Rtt109 residues do not participate in Asf1-mediated Rtt109 acetylation in vitro or H3K56 acetylation in yeast cells, demonstrating that Asf1 and Vps75 dictate Rtt109 substrate specificity through distinct mechanisms. These studies also suggest that Vps75 binding stimulates Rtt109 catalytic activity by appropriately presenting the H3-H4 substrate within the central cavity of the holoenzyme to promote H3K9/K27 acetylation of new histones before deposition.

PubMed: 21256037
DOI: 10.1016/j.str.2010.12.012

Experimental method

X-RAY DIFFRACTION (2.8 Å)