ArticleTraffic (Copenhagen, Denmark)2011
Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo.
Article in Traffic (Copenhagen, Denmark), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4.Life science alliance · 2020Article
- Histone chaperone exploits intrinsic disorder to switch acetylation specificity.Nature communications · 2019Article
- Chaperoning RPA during DNA metabolism.Current genetics · 2019Review
- Ccp1 modulates epigenetic stability at centromeres and affects heterochromatin distribution inThe Journal of biological chemistry · 2018Article
- The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.Nucleic acids research · 2016Article
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- Cell cycle-dependent changes in H3K56ac in human cells.Cell cycle (Georgetown, Tex.) · 2015Article
- Characterization of the Pneumocystis carinii histone acetyltransferase chaperone proteins PcAsf1 and PcVps75.Infection and immunity · 2013Article
- The carboxyl terminus of Rtt109 functions in chaperone control of histone acetylation.Eukaryotic cell · 2013Article
- Chaperone-mediated acetylation of histones by Rtt109 identified by quantitative proteomics.Journal of proteomics · 2013Article
- Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation.Molecular and cellular biology · 2013Article
- All roads lead to chromatin: Multiple pathways for histone deposition.Biochimica et biophysica acta · 2012Article
- Histone chaperones link histone nuclear import and chromatin assembly.Biochimica et biophysica acta · 2012Article
- Understanding histone acetyltransferase Rtt109 structure and function: how many chaperones does it take?Current opinion in structural biology · 2011Review
- Structural basis for the acetylation of histone H3K9 and H3K27 mediated by the histone chaperone Vps75 inSignal transduction and targeted therapyArticle
- Histone-modifying enzymes, histone modifications and histone chaperones in nucleosome assembly: Lessons learned from Rtt109 histone acetyltransferases.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Modification of histones is critical for the regulation of all chromatin-templated processes. Yeast Rtt109 is a histone acetyltransferase (HAT) that acetylates H3 lysines 9, 27 and 56. Rtt109 associates with and is stabilized by Nap1 family histone chaperone Vps75. Our data suggest Vps75 and Nap1 have some overlapping functions despite their different cellular localization and histone binding specificity. We determined that Vps75 contains a classical nuclear localization signal and is imported by Kap60-Kap95. Rtt109 nuclear localization depends on Vps75, and nuclear localization of the Vps75-Rtt109 complex is not critical for Rtt109-dependent functions, suggesting Rtt109 may be able to acetylate nascent histones before nuclear import. To date, the effects of VPS75 deletion on Rtt109 function had not been separated from the resulting Rtt109 degradation; thus, we used an Rtt109 mutant lacking the Vps75-interaction domain that is stable without Vps75. Our data show that in addition to promoting Rtt109 stability, Vps75 binding is necessary for Rtt109 acetylation of the H3 tail. Direct interaction of Vps75 with H3 likely allows Rtt109 access to the histone tail. Furthermore, our genetic interaction data support the idea of Rtt109-independent functions of Vps75. In summary, our data suggest that Vps75 influences chromatin structure by regulating histone modification and through its histone chaperone functions.
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