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SRX13211274: GSM5702083: ACSS2, Log Growth Replicate 2; Saccharomyces cerevisiae; ChIP-Seq
1 ILLUMINA (NextSeq 550) run: 11M spots, 835.3M bases, 319.2Mb downloads

Submitted by: NCBI (GEO)
Study: Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites (ChIP-Seq)
show Abstracthide Abstract
Histone acetylation, a post-translational modification associated with transcriptional activation, is governed by nuclear acetyl-CoA pools that can vary depending on the metabolic state of the cell. The metabolic enzyme acetyl-CoA synthetase 2 (ACSS2) is proposed to regulate nuclear acetyl-CoA levels, using local acetate to produce acetyl-CoA that is utilized for histone acetylation. We hypothesize that during gene activation, a local transfer of intact acetate occurs between histones to upregulate transcription via sequential action of epigenetic and metabolic enzymes. Here we present converging lines of evidence in support of this acetate transfer to serve rapid gene induction. Using stable isotope labeling, we detect local transfer of intact acetate between histone acetylation sites both in vitro using purified mammalian enzymes and in vivo using quiescence exit in Saccharomyces cerevisiae as a change-of-state model. We delineate the enzymatic components required for this transfer mechanism, finding that ACSS2, histone deacetylase and histone acetyltransferase enzymes are necessary for efficient acetyl-group transfer in vitro. We show that Acs2, the yeast orthologue of ACSS2, is recruited to the genome during quiescence exit, and observe dynamic changes of histone acetylation in the vicinity of Acs2 peaks in vivo. Strikingly, we find that Acs2 is preferentially associated with the most upregulated growth genes, suggesting that acetyl-group transfer might play an important role in increased gene expression. Overall, our data reveal direct transfer of acetate between histone lysine residues to facilitate rapid transcriptional induction, an exchange that may be critical during metabolic alterations and changes in nutrient availability. Overall design: ChIP-seq in a time-course in S. cerevisiae during quiescence exit, measuring four histone acetylation post-translational modifications (H3K9ac, H3K18ac, H3K23ac, and H3K27ac) as well as the enzyme ACSS2; ACSS2 is also measured using TAP-tag in a second strain of yeast. Four time points are measured: glucose-deprived quiescent cells (Q), 30 min post-quiescence exit (E30), 240 min post-quiescence exit (E240), and logarithmic growth (LOG). The replicate structure is as follows: H3K9ac, H3K18ac, H3K23ac, H3K27ac and non-tagged ACSS2 have two replicates each in each time point, with a corresponding two replicates of input in each time point to adjust for sonication efficiency bias; while TAP-tagged ACSS2 has two replicates in Q and E30 and one sample in E240 and LOG, with a corresponding input from this strain with identical replicate structure.
Sample: ACSS2, Log Growth Replicate 2
SAMN23413123 • SRS11137325 • All experiments • All runs
Library:
Instrument: NextSeq 550
Strategy: ChIP-Seq
Source: GENOMIC
Selection: ChIP
Layout: SINGLE
Construction protocol: Cultures were cross-linked with 1% formaldehyde at RT for 10 min. Reaction was stopped by adding 135 mM glycine. Cultures were then pelleted, washed and resuspended in FA-lysis buffer containing protease/phosphatase inhibitors and 10 mM Na-butyrate. Cells were lysed using a 0.5 mm Zirconia/Silica beads (RPI #9834) in a Mini-Beadbeater high energy cell disruptor (BioSpec) at 4°C, for 6 times 60 seconds. Samples were cooled on ice for 2 min in-between beatings. Subsequently, lysates were sonicated for 20 min in BioRuptor (Diagenode), using high setting and 30 seconds ON/OFF cycles. Cell debris was removed by centrifugation at 10,000 rcf for 15 min at 4°C. Sonication efficiency was confirmed for each sample by running on 0.8% agarose gel. Equal aliquots of sonicated lysates were used per immunoprecipitation reaction with 5 ul of H3K9ac antibody (Active Motif 39317), 5 ul H3K14ac antibody (Active Motif 39697), 5 ul of H3K18ac antibody (Active Motif 39755), 4 ul H3K23ac antibody (Millipore 07-355), 5 ul H3K27ac antibody (Abcam ab4729), 5 ul of H4K12ac antibody (Abcam ab46983), 5 ul H4K16ac antibody (Millipore 07-329), 5 ul Acs2 antibody (Thermo MA5-14810) or 8 ul TAP antibody (Invitrogen CAB1001) preconjugated to Protein G Dynabeads (Life Technologies). Ten percent of the chromatin was saved as input DNA. ChIP reactions were incubated overnight at 4 °C with rotation and washed three times in wash buffer. Immunoprecipitated DNA was eluted from the beads, reversed cross-linked and purified together with the input DNA. Exactly 20 ng DNA (either ChIP or input) was used to construct sequencing libraries using the NEBNext Ultra II DNA library preparation kit for Illumina (New England Biolabs; NEB). Libraries were multiplexed using NEBNext Multiplex Oligos for Illumina (dual index primers) and single-end sequenced (75 bp) on the NextSeq 550 platform (Illumina) in accordance with the manufacturer's protocol.
Experiment attributes:
GEO Accession: GSM5702083
Links:
Runs: 1 run, 11M spots, 835.3M bases, 319.2Mb
Run# of Spots# of BasesSizePublished
SRR1702124011,041,029835.3M319.2Mb2022-01-23

ID:
18071935

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