PXD011365-1

PXD011365 is an original dataset announced via ProteomeXchange.

Title	Effects of hypoxia-reoxygenation stress on mitochondrial proteome and bioenergetics of the hypoxia-tolerant marine bivalve Crassostrea gigas
Description	Intermittent hypoxia is a common stressor in estuarine and coastal habitats due to the diurnal and tidal cycles of oxygen availability. Oxygen deficiency results in energy stress by limiting aerobic ATP production, while reoxygenation may lead to oxidative injury due to the excessive production of reactive oxygen species (ROS) in mitochondria. Mitochondria are a key intracellular target of hypoxia-reoxygenation (H/R) stress due to their central role in ATP production, ROS generation and stress signaling. Marine intertidal bivalves such as the Pacific oyster Crassostrea gigas are adapted to frequent H/R cycles in the intertidal zone and maintain mitochondrial integrity and aerobic function despite frequent oxygen fluctuations. To gain insight into the molecular responses of mitochondria of the hypoxia-tolerant Pacific oyster to H/R stress, we studied changes in oxidative phosphorylation (OXPHOS) capacity, proton leak and activity of the electron transport system enzymes (ETS) in gill mitochondria of C. gigas. We furthermore investigated shifts in mitochondrial proteome and phosphoproteome after 24 h of hypoxia and 1 h of post-hypoxic recovery. Oyster mitochondria maintained normal ETS and OXPHOS capacity during H/R stress, despite a slight but significant decline in cytochrome c oxidase (Complex IV) activity after reoxygenation. Fifty total proteins and 36 phosphoproteins were differentially abundant in mitochondria of H/R exposed oysters compared with the controls. Rearrangements of the mitochondrial (phospho)proteome during H/R stress involved upregulation of mitochondrial ETS (most notably Complexes I and IV) and iron-binding proteins (frataxin and ferrochelatase) as well as suppression of the metabolic pathways that channel electrons to ubiquinone, possibly as a mechanism to limit ROS production due to the iron overload and reverse flow of electrons through ETS. H/R stress also led to upregulation of a mitophagic activator serine/threonine protein phosphatase PGAM5 and dephosphorylation of metalloendopeptidase OMA1 indicating stimulation of mitochondrial quality control mechanisms during reoxygenation. Changes in the overall abundance and phosphorylation levels of several key proteins involved in the mitochondrial protein homeostasis (including subunits of the mitochondrial ribosome, mitochondrial inner membrane translocase and elongation factor G) are consistent with the suppression of the protein synthesis during hypoxia, likely as an energy-saving mechanism. Overall, our study indicates that shifts in the mitochondrial (phospho-)proteome play an important role in responses of oysters to H/R stress and might complement adaptations of anaerobic metabolism and metabolic rate depression in ensuring hypoxic survival and rapid recovery in this hypoxia-tolerant intertidal species.
HostingRepository	PRIDE
AnnounceDate	2021-11-04
AnnouncementXML	Submission_2021-11-04_00:32:13.131.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD011365
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Stephanie Markert
SpeciesList	scientific name: Crassostrea gigas (Pacific oyster) (Crassostrea angulata); NCBI TaxID: 29159;
ModificationList	Oxidation; Carbamidomethyl
Instrument	LTQ Orbitrap Classic; LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2018-10-15 23:43:27	ID requested
⏵ 1	2021-11-04 00:32:13	announced
2	2024-10-22 05:30:16	announced	2024-10-22: Updated project metadata.

Sokolov EP, Markert S, Hinzke T, Hirschfeld C, Becher D, Ponsuksili S, Sokolova IM, Effects of hypoxia-reoxygenation stress on mitochondrial proteome and bioenergetics of the hypoxia-tolerant marine bivalve Crassostrea gigas. J Proteomics, 194():99-111(2019) [pubmed]

curator keyword: Biological

submitter keyword: Oyster, mitochondria, hypoxia/reoxygenation, LC-MS/MS, proteomics

Stephanie Markert
contact affiliation	Universität Greifswald Institut für Pharmazie, AG Pharmazeutische Biotechnologie Greifswald, Germany
contact email	stephanie.markert@uni-greifswald.de
lab head
Stephanie Markert
contact affiliation	University of Greifswald
contact email	stephanie.markert@uni-greifswald.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD011365
     1. Label: PRIDE project
     2. Name: Effects of hypoxia-reoxygenation stress on mitochondrial proteome and bioenergetics of the hypoxia-tolerant marine bivalve Crassostrea gigas