Proteomics,Multiomics

Dataset Information

0

Protein acetylation in young versus midlife Drosophila male heads

ABSTRACT: Old age is associated with a progressive decline of mitochondrial function and changes in nuclear chromatin. However, little is known about how metabolic activity and epigenetic modifications change as organisms reach their midlife. Here, we assessed how protein acetylation changes during midlife in Drosophila melanogaster. Midlife flies show elevated acetyl-CoA levels and alterations in protein acetylation. Based on these observations, we decreased the activity of the acetyl-CoA-synthesizing enzyme ATP citrate lyase (ATPCL). We find that lower ATPCL activity alleviates the observed aging-associated changes and promote longevity. Our findings reveal a pathway that couples changes of intermediate metabolism during aging with the chromatin-mediated regulation of transcription and changes in the activity of associated enzymes that modulate organismal lifespan.

OTHER RELATED OMICS DATASETS IN: PRJNA302813

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

TISSUE(S): Head

SUBMITTER: Ignasi Forne  

LAB HEAD: Axel Imhof

PROVIDER: PXD003318 | Pride | 2016-01-22

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
AcetylKSitessample5youngversusmidlife.txt Txt
AcetylKSitessamples1-4youngversusmidlife.txt Txt
F_Acetylationenrichment_1midlife_.RAW Raw
F_Acetylationenrichment_1young_.RAW Raw
F_Acetylationenrichment_2midlife_.RAW Raw
Items per page:
1 - 5 of 24
altmetric image

Publications

Old age is associated with a progressive decline of mitochondrial function and changes in nuclear chromatin. However, little is known about how metabolic activity and epigenetic modifications change as organisms reach their midlife. Here, we assessed how cellular metabolism and protein acetylation change during early aging in Drosophila melanogaster. Contrary to common assumptions, we find that flies increase oxygen consumption and become less sensitive to histone deacetylase inhibitors as they  ...[more]

Similar Datasets

Genomics Genome wide H3K9ac and SAGA occupancy at OX growth phase and RC quiescent phase of yeast metabolic cycle
2011-05-19 | E-GEOD-28734 | biostudies-arrayexpress
Transcriptomics Cytosolic acetyl-CoA promotes histone acetylation predominantly at H3K27 in Arabidopsis
2017-09-25 | GSE79524 | GEO
Genomics Metabolic dependencies of metastasis-initiating cells in breast cancer [ChIP-Seq]
2023-09-20 | GSE236223 | GEO
Proteomics Characterization of lysine acetylation in Toxoplasma gondii proteome lacking acetyl-CoA transporter 1 (AT1).
2022-07-25 | PXD030932 | Pride
Genomics Acetyl-CoA production by Mediator-bound 2-ketoacid dehydrogenases boosts de novo histone acetylation and is regulated by nitric oxide [Chipseq_MED1_RAW2647]
2024-11-19 | GSE245579 | GEO
Transcriptomics Acetyl-CoA production by Mediator-bound 2-ketoacid dehydrogenases boosts de novo histone acetylation and is regulated by nitric oxide [Chrom_RNAseq_iNOS1400W]
2024-11-19 | GSE245445 | GEO
Genomics Acetyl-CoA production by Mediator-bound 2-ketoacid dehydrogenases boosts de novo histone acetylation and is regulated by nitric oxide [Chipseq_panAc_spikein]
2024-11-19 | GSE245444 | GEO
Genomics Acetyl-CoA production by Mediator-bound 2-ketoacid dehydrogenases boosts de novo histone acetylation and is regulated by nitric oxide [Chipseq_MED1_HELA]
2024-11-19 | GSE245443 | GEO
Genomics Acetyl-CoA production by Mediator-bound 2-ketoacid dehydrogenases boosts de novo histone acetylation and is regulated by nitric oxide [Chipseq_H3K27ac_spikein]
2024-11-19 | GSE245442 | GEO
Genomics Acetyl-CoA production by Mediator-bound 2-ketoacid dehydrogenases boosts de novo histone acetylation and is regulated by nitric oxide [Chipseq_FLAG_DLST_ODGH]
2024-11-19 | GSE245441 | GEO