| Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4. | Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4.
Akhavantabib N, Krzizike DD, Neumann V, D'Arcy S., Free PMC Article | 07/17/2021 |
| he model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer. | The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.
Hammond CM, Sundaramoorthy R, Larance M, Lamond A, Stevens MA, El-Mkami H, Norman DG, Owen-Hughes T., Free PMC Article | 06/10/2017 |
| Vps75 and Asf1 both enhance Rtt109 acetylation for H3/H4 | Utilizing targeted mass spectrometry to demonstrate Asf1-dependent increases in residue specificity for Rtt109-Vps75 mediated histone acetylation.
Kuo YM, Henry RA, Huang L, Chen X, Stargell LA, Andrews AJ., Free PMC Article | 02/6/2016 |
| Rtt109-Vps75 preferentially acetylates H3 K9 and K23 | Chaperone-mediated acetylation of histones by Rtt109 identified by quantitative proteomics.
Abshiru N, Ippersiel K, Tang Y, Yuan H, Marmorstein R, Verreault A, Thibault P., Free PMC Article | 09/14/2013 |
| findings show that Nap1 and Vps75 regulate cryptic transcription observed in the absence of Ctk1. Rtt109 acetylation of H3 K9 also plays a role in this pathway, and both Vps75 and Nap1 promote acetylation of H3 in the ORF. | Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation.
Xue YM, Kowalska AK, Grabowska K, Przybyt K, Cichewicz MA, Del Rosario BC, Pemberton LF., Free PMC Article | 06/15/2013 |
| Data show that Rtt109 nuclear localization depends on Vps75, and nuclear localization of the Vps75-Rtt109 complex is not critical for Rtt109-dependent functions. | Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo.
Keck KM, Pemberton LF., Free PMC Article | 10/8/2011 |
| Histone chaperones, Vps75 or Asf1, dictate Histone acetyltransferase, Rtt109, substrate specificity through distinct mechanisms. | Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation.
Tang Y, Holbert MA, Delgoshaie N, Wurtele H, Guillemette B, Meeth K, Yuan H, Drogaris P, Lee EH, Durette C, Thibault P, Verreault A, Cole PA, Marmorstein R., Free PMC Article | 07/2/2011 |
| the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109. | Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex.
Su D, Hu Q, Zhou H, Thompson JR, Xu RM, Zhang Z, Mer G., Free PMC Article | 07/2/2011 |
| Results indicate a role for Vps75 in nucleosome dynamics during transcription, and importantly, this function appears to be largely independent of Rtt109. | An rtt109-independent role for vps75 in transcription-associated nucleosome dynamics.
Selth LA, Lorch Y, Ocampo-Hafalla MT, Mitter R, Shales M, Krogan NJ, Kornberg RD, Svejstrup JQ., Free PMC Article | 01/21/2010 |
| probed the molecular functions of Vps75 and the Rtt109-Vps75 complex through biochemical, structural and genetic means | Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75.
Berndsen CE, Tsubota T, Lindner SE, Lee S, Holton JM, Kaufman PD, Keck JL, Denu JM., Free PMC Article | 01/21/2010 |
| two surfaces on the earmuff domain of Vps75 participate in Rtt109 interaction with a stoichiometry of 2:1 | Structure of Vps75 and implications for histone chaperone function.
Tang Y, Meeth K, Jiang E, Luo C, Marmorstein R., Free PMC Article | 01/21/2010 |
| one function of the Rtt109-Vps75 interacting protein pair is to affect the efficiency of NHEJ in yeast | Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae.
Jessulat M, Alamgir M, Salsali H, Greenblatt J, Xu J, Golshani A. | 01/21/2010 |