title: Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation.
abstract: Histone chaperones function in chromatin assembly and disassembly, suggesting they have important regulatory roles in transcription elongation. The Saccharomyces cerevisiae proteins Nap1 and Vps75 are structurally related, evolutionarily conserved histone chaperones. We showed that Nap1 genetically interacts with several transcription elongation factors and that both Nap1 and Vps75 interact with the RNA polymerase II kinase, CTK1. Loss of NAP1 or VPS75 suppressed cryptic transcription within the open reading frame (ORF) observed when strains are deleted for the kinase CTK1. Loss of the histone acetyltransferase Rtt109 also suppressed ctk1-dependent cryptic transcription. Vps75 regulates Rtt109 function, suggesting that they function together in this process. Histone H3 K9 was found to be the important lysine that is acetylated by Rtt109 during ctk1-dependent cryptic transcription. We showed that both Vps75 and Nap1 regulate the relative level of H3 K9 acetylation in the STE11 ORF. This supports a model in which Nap1, like Vps75, directly regulates Rtt109 activity or regulates the assembly of acetylated chromatin. Although Nap1 and Vps75 share many similarities, due to their distinct interactions with SET2, Nap1 and Vps75 may also play separate roles during transcription elongation. This work sheds further light on the importance of histone chaperones as general regulators of transcription elongation.
authors: Department of Microbiology, Immunology and Cancer Biology, Center for Cell Signaling, University of Virginia, Charlottesville, Virginia, USA.
authors: Yu-Ming
authors: YM
authors: Xue
authors: Anna K
authors: AK
authors: Kowalska
authors: Kamila
authors: K
authors: Grabowska
authors: Katarzyna
authors: K
authors: Przybyt
authors: Magda A
authors: MA
authors: Cichewicz
authors: Brian C
authors: BC
authors: Del Rosario
authors: Lucy F
authors: LF
authors: Pemberton
mesh_terms: D000107:Acetylation; D042002:Chromatin Assembly and Disassembly; D051548:Histone Acetyltransferases / Q000235:genetics; D056488:Histone Chaperones; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D020930:MAP Kinase Kinase Kinases / Q000378:metabolism; D008780:Methyltransferases / Q000378:metabolism; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D056490:Nucleosome Assembly Protein 1 / Q000235:genetics / Q000378:metabolism*; D016366:Open Reading Frames; D011494:Protein Kinases / Q000235:genetics* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: C118305:CTDK-I protein complex, S cerevisiae; D056488:Histone Chaperones; D006657:Histones; D018832:Molecular Chaperones; C533556:NAP1 protein, S cerevisiae; D056490:Nucleosome Assembly Protein 1; D029701:Saccharomyces cerevisiae Proteins; C525548:Vps75 protein, S cerevisiae; D008780:Methyltransferases; C448996:Set2 protein, S cerevisiae; D051548:Histone Acetyltransferases; C517120:Rtt109 protein, S cerevisiae; D011494:Protein Kinases; D020930:MAP Kinase Kinase Kinases; C067018:Ste11 protein, S cerevisiae
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