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Qi"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry"],"software":[""],"submitter_keywords":["H3k79me3  h3t11 phosphorylation  histone homeostasis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077347"],"sample_protocol":["Yeast strains Hat-Flag, Atg19-Flag, Cac1-Flag, Cac2-Flag, H3-Flag and Asf1-Flag was harvested from 1 liter culture cultured in rich media overnight to an optical density at 600 (OD600) of 1.0, washed and flash frozen in liquid nitrogen. Thawed cell pellets were ground with glass beads by using a Biospec bead beater [30 sec ON, 90 sec OFF] in for 70 min in H350 buffer (25 mM Hepes-KOH pH7.6, 0.5 mM EDTA. 0.02% NP40, 350 mM KCl, 2 mM MgCl2, 10 % glycerol, 1 mM PMSF, 2 μg/mL leupeptin, 50 mM NaF, 1mM Na3VO4). The lysate was cleared by centrifugation at 45,000 rpm at 4ºC for 1.5 h and the supernatant was incubated with anti-FLAG M2 affinity gel (Sigma) at 4ºC for 8 h. The beads were washed extensively in H350 buffer and the immunoprecipitated proteins were disulphide-reduced by 25 mM DTT at 37℃ for 40 min. Cysteines were alkylated by 50 mM iodoacetamide in the dark for 30 min. The immunoprecipitated proteins were digested overnight with sequencing-grade trypsin (Promega) at 37℃ and desalted using C18 columns (Thermo Fisher) and lyophilized. The dried peptides were reconstituted in 0.1% FA and loaded onto an Acclaim PepMap 100 C18 LC column (Thermo Fisher) utilizing a Thermo Easy nLC 1000 LC system (Thermo Fisher) connected to QEHF Orbitrap mass spectrometer (Thermo). The raw mass spectrometry data were searched against the Saccharomyces cerevisiae proteome database from Uniport (https://www.uniprot.org/proteomes/UP000002311) using Sequest HT, MS Amanda and ptmRS algorithms in Proteome Discoverer 3.1 (Thermo Fisher). For Asf1-FLAG and H3-FLAg affinity MS, peptides was digested by mass spectrum grade trypsin Lys-C (Promega VA1170) at 37 ℃ water bath overnight and desalted using C18 columns (Thermo Fisher) and lyophilized. The dried peptides were reconstituted in 0.1% FA and loaded onto an Acclaim PepMap 100 C18 LC column (Thermo Fisher) utilizing a Thermo Easy nLC 1000 LC system (Thermo Fisher) connected to QEHF Orbitrap mass spectrometer (Thermo) with a data independent acquisition (DIA) model. The DIA data was analyzed by DIA-NN software and phosphorylation was considered as variant modification with a parameter of --var-mod UniMod:21,79.966331,STY. The MS/MS spectrum was visualized by Skyline software as instructed."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The dried peptides were reconstituted in 0.1% formic acid  and loaded onto an Acclaim PepMap 100 C18 LC column (Thermo Fisher) utilizing a Thermo Easy nLC 1000 LC system (Thermo Fisher) connected to Thermo Q Exactive HF mass spectrometer (Thermo). The peptides were eluted with a 5–20% gradient of acetonitrile with 0.1% formic acid over 70 min with a flow rate of 300 nl min−1. The MS1 scans were performed at a resolution of 60,000 over a mass range of 380–1,560 m/z, with a maximum injection time of 120 ms and an AGC target of 1 × 106. The MS2 scans were performed at a resolution of 15,000, with the normalized collision energy set to 24, a maximum injection time of 50 ms and an AGC target of 2 × 105. Determination of phosphorylation sites using mass spectrometry refers to previous research [1]. The raw mass spectrometry data were searched against the Saccharomyces cerevisiae proteome database from Uniport (https://www.uniprot.org/proteomes/UP000002311) using Sequest HT, MS Amanda and ptmRS algorithms in Proteome Discoverer 2.3 (Thermo Fisher). The precursor ion mass tolerance was set to 10 ppm and the fragment ion mass was 0.02 Da. Dynamic modifications were set for methionine oxidation and phosphorylation on serine, threonine and tyrosine. Only fully tryptic peptides with up to two mis-cleavages and a false-detection rate of 1% using the percolator validator algorithms were accepted."],"omics_type":["Proteomics"],"labhead":["Yu qi"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["School of Life Sciences, Hubei University, Wuhan, Hubei 430062, China"],"species":["Saccharomyces Cerevisiae (baker's Yeast)"],"publication":["Not available"],"submitter_mail":["yuqi195316@outlook.com"],"submitter_affiliation":["hubei university"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"H3pT11 regulates histone homeostasis and replication-coupled nucleosome assembly","description":"newly synthesized H3 is phosphorylated at T11 by the CPC complex, licensing Asf1 binding and nuclear import; upon nuclear entry, H3pT11 facilitates Rtt109-catalyzed H3K56 acetylation, which antagonizes Hat1 and promotes nucleosome assembly by CAF-1 and Rtt106 16; subsequently, Rtt101-mediated H3K122 ubiquitination destabilizes the Asf1-H3/H4 interaction, enabling dimer transfer from Asf1 to 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