ArticleInfection and immunity2013
Characterization of the Pneumocystis carinii histone acetyltransferase chaperone proteins PcAsf1 and PcVps75.
Article in Infection and immunity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation.Nucleic acids research · 2019Article
- Characterization of N-Acetylglucosamine Biosynthesis in Pneumocystis species. A New Potential Target for Therapy.American journal of respiratory cell and molecular biology · 2017Article
- Article
- Pneumocystis.Cold Spring Harbor perspectives in medicine · 2014Review
- Pneumocystis jirovecii Rtt109, a novel drug target for Pneumocystis pneumonia in immunosuppressed humans.Antimicrobial agents and chemotherapy · 2014Article
- A cell-free fluorometric high-throughput screen for inhibitors of Rtt109-catalyzed histone acetylation.PloS one · 2013Article
- Histone-modifying enzymes, histone modifications and histone chaperones in nucleosome assembly: Lessons learned from Rtt109 histone acetyltransferases.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Rtt109 is a lysine acetyltransferase that acetylates histone H3 at lysine 56 (H3K56) in fungi. This acetylation event is important for proper DNA replication and repair to occur. Efficient Rtt109 acetyltransferase activity also requires a histone chaperone, vacuolar protein sorting 75 (Vps75), as well as the major chaperone of the H3-H4 dimer, anti-silencing factor 1 (Asf1). Little is known about the role of these proteins in the opportunistic fungal pathogen Pneumocystis carinii. To investigate the functions of Asf1 and Vps75 in Pneumocystis carinii, we cloned and characterized both of these genes. Here, we demonstrate that both genes, P. carinii asf1 (Pcasf1) and Pcvps75, function in a fashion analogous to their Saccharomyces cerevisiae counterparts. We demonstrate that both P. carinii Asf1 (PcAsf1) and PcVps75 can bind histones. Furthermore, when Pcasf1 is expressed heterologously in S. cerevisiae asf1Δ cells, PcAsf1 can restore full H3 lysine acetylation. We further demonstrated that the Pcasf1 cDNA expressed in asf1Δ S. cerevisiae cells can restore growth to wild-type levels in the presence of genotoxic agents that block DNA replication. Lastly, we observed that purified PcAsf1 and PcVps75 proteins enhance the ability of PcRtt109 to acetylate histone H3-H4 tetramers. Together, our results indicate that the functions of the Rtt109-Asf1-Vps75 complex in the acetylation of histone H3 lysine 56 and in DNA damage response are present in P. carinii DNA and cell cycle progression.
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