Dataset Information

Mitochondrial ADP-ribosylation regulates NAD+-dependent genotoxic stress responses

ABSTRACT: ADP-ribosylome analysis in human U20S cells and mouse muscle tissues

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Skeletal Muscle Fiber

SUBMITTER: Deena Leslie Pedrioli

LAB HEAD: Michael O. Hottiger

PROVIDER: PXD013918 | Pride | 2021-09-08

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20180709_04_DLP116_AFWT_WT1.raw	Raw
	20180709_04_DLP116_AFWT_WT1_etd_no_diag_sep.prot.xls	Xls
	20180709_04_DLP116_AFWT_WT1_hcd35_no_diag_sep.prot.xls	Xls
	20180709_08_DLP116_AFWT_WT3.raw	Raw
	20180709_08_DLP116_AFWT_WT3_etd_no_diag_sep.prot.xls	Xls

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Publications

Mitochondrial NAD+ Controls Nuclear ARTD1-Induced ADP-Ribosylation.

Hopp Ann-Katrin AK Teloni Federico F Bisceglie Lavinia L Gondrand Corentin C Raith Fabio F Nowak Kathrin K Muskalla Lukas L Howald Anna A Pedrioli Patrick G A PGA Johnsson Kai K Altmeyer Matthias M Pedrioli Deena M Leslie DML Hottiger Michael O MO

Molecular cell 20210114 2

In addition to its role as an electron transporter, mitochondrial nicotinamide adenine dinucleotide (NAD+) is an important co-factor for enzymatic reactions, including ADP-ribosylation. Although mitochondria harbor the most intra-cellular NAD+, mitochondrial ADP-ribosylation remains poorly understood. Here we provide evidence for mitochondrial ADP-ribosylation, which was identified using various methodologies including immunofluorescence, western blot, and mass spectrometry ...[more]

PMID: 33450210

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Project description:To achieve the extreme nuclear condensation necessary for sperm function, most histones are replaced with protamines during spermiogenesis in mammals. Mature sperm retain only a small fraction of nucleosomes, which are, in part, enriched on gene regulatory sequences, and recent findings suggest that these retained histones provide epigenetic information that regulates expression of a subset of genes involved in embryo development after fertilization. We addressed this tantalizing hypothesis by analyzing two mouse models exhibiting abnormal histone positioning in mature sperm due to impaired poly(ADP-ribose) (PAR) metabolism during spermiogenesis and identified altered sperm histone retention in specific gene loci genome-wide using MNase digestion-based enrichment of mononucleosomal DNA. We then set out to determine the extent to which expression of these genes was altered in embryos generated with these sperm. For control sperm, most genes showed some degree of histone association, unexpectedly suggesting that histone retention in sperm genes is not an all-or-none phenomenon and that a small number of histones may remain associated with genes throughout the genome. The amount of retained histones, however, was altered in many loci when PAR metabolism was impaired. To ascertain whether sperm histone association and embryonic gene expression are linked, the transcriptome of individual 2-cell embryos derived from such sperm was determined using microarrays and RNA sequencing. Strikingly, a moderate but statistically significant portion of the genes that were differentially expressed in these embryos also showed different histone retention in the corresponding gene loci in sperm of their fathers. These findings provide new evidence for the existence of a linkage between sperm histone retention and gene expression in the embryo. Mnase sensitivity of sperm DNA, indicating nucleosomal, not protamine, packaging was altered in mice by manipulating poly(ADP-ribose) metabolism in adult males using a specific PARP inhibitor for 6 weeks. Abnormal sperm nucleosomal organization of males analyzed by these tiling arrays was compared with differential gene expression in 2 cell embryos fathered by these males analyzed by separate gene expression arrays and RNA sequencing.

Dataset Information

Mitochondrial ADP-ribosylation regulates NAD+-dependent genotoxic stress responses

Dataset's files

Publications

Mitochondrial NAD<sup>+</sup> Controls Nuclear ARTD1-Induced ADP-Ribosylation.

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