Data_Sheet_7_The Role of Reversible Protein Phosphorylation in Regulation of the Mitochondrial Electron Transport System During Hypoxia and Reoxygenation Stress in Marine Bivalves.PDF
Fluctuations in the ambient oxygen concentrations represent a major stressor for aerobic organisms causing ATP deficiency during hypoxia and excessive production of reactive oxygen species during reoxygenation. Modulation of the mitochondrial electron transport system activity was proposed as a majo...
Main Authors: | , , , |
---|---|
Format: | Dataset |
Language: | unknown |
Published: |
2020
|
Subjects: | |
Online Access: | https://doi.org/10.3389/fmars.2020.00467.s007 https://figshare.com/articles/dataset/Data_Sheet_7_The_Role_of_Reversible_Protein_Phosphorylation_in_Regulation_of_the_Mitochondrial_Electron_Transport_System_During_Hypoxia_and_Reoxygenation_Stress_in_Marine_Bivalves_PDF/12598877 |
id |
ftfrontimediafig:oai:figshare.com:article/12598877 |
---|---|
record_format |
openpolar |
spelling |
ftfrontimediafig:oai:figshare.com:article/12598877 2023-05-15T15:18:38+02:00 Data_Sheet_7_The Role of Reversible Protein Phosphorylation in Regulation of the Mitochondrial Electron Transport System During Hypoxia and Reoxygenation Stress in Marine Bivalves.PDF Halina I. Falfushynska Eugene Sokolov Helen Piontkivska Inna M. Sokolova 2020-07-02T04:22:21Z https://doi.org/10.3389/fmars.2020.00467.s007 https://figshare.com/articles/dataset/Data_Sheet_7_The_Role_of_Reversible_Protein_Phosphorylation_in_Regulation_of_the_Mitochondrial_Electron_Transport_System_During_Hypoxia_and_Reoxygenation_Stress_in_Marine_Bivalves_PDF/12598877 unknown doi:10.3389/fmars.2020.00467.s007 https://figshare.com/articles/dataset/Data_Sheet_7_The_Role_of_Reversible_Protein_Phosphorylation_in_Regulation_of_the_Mitochondrial_Electron_Transport_System_During_Hypoxia_and_Reoxygenation_Stress_in_Marine_Bivalves_PDF/12598877 CC BY 4.0 CC-BY Oceanography Marine Biology Marine Geoscience Biological Oceanography Chemical Oceanography Physical Oceanography Marine Engineering hypoxia reoxygenation post-translational modification (PTM) mitochondrial electron transport chain (ETC) Mollusca respiratory complexes NADH:ubiquinone oxidoreductase cytochrome c oxidase Dataset 2020 ftfrontimediafig https://doi.org/10.3389/fmars.2020.00467.s007 2020-07-08T22:56:08Z Fluctuations in the ambient oxygen concentrations represent a major stressor for aerobic organisms causing ATP deficiency during hypoxia and excessive production of reactive oxygen species during reoxygenation. Modulation of the mitochondrial electron transport system activity was proposed as a major mechanism involved in both the mitochondrial injury and adaptive response, but the mechanisms of ETS regulation during hypoxia/reoxygenation (H/R) stress remain poorly understood in hypoxia-tolerant organisms. To address this gap, we focused on the effects of H/R on activities of the mitochondrial Complexes I and IV in hypoxia-tolerant marine bivalves, the blue mussel Mytilus edulis, the Arctic quahog Arctica islandica and the Pacific oyster Crassostrea gigas, exposing them for 1 or 6 days to extreme hypoxia (<0.1% O 2 ) followed by 1 h of reoxygenation. We used a combination of bioinformatics analysis, biochemical and molecular studies to examine the potential role of the reversible protein phosphorylation in regulation of the Complex I and IV activities and in the mitochondrial responses to H/R stress. Our results showed a strong species-specific modulation of two important kinases, the serine/threonine protein kinase A (PKA) and protein kinase C (PKC) by H/R stress in the studied bivalves. The mitochondrial Complexes I and IV emerged as important targets for modulation by H/R stress, mediated in part through reversible phosphorylation by PKA and PKC. The effects of the reversible phosphorylation on the enzyme activities were species- and condition-specific. In mussels and quahogs, phosphorylation by PKA and PKC led to a strong increase in activity of Complexes I and IV. In oysters, Complexes I and IV were insensitive to PKA and PKC activation except after prolonged hypoxia and reoxygenation when elevated sensitivity to PKA and PKC activation indicated a change in the configuration and/or isoform composition of these enzymes. Non-site-specific dephosphorylation strongly suppressed the activity of Complex I and ... Dataset Arctic Arctica islandica Crassostrea gigas Pacific oyster Frontiers: Figshare Arctic Pacific |
institution |
Open Polar |
collection |
Frontiers: Figshare |
op_collection_id |
ftfrontimediafig |
language |
unknown |
topic |
Oceanography Marine Biology Marine Geoscience Biological Oceanography Chemical Oceanography Physical Oceanography Marine Engineering hypoxia reoxygenation post-translational modification (PTM) mitochondrial electron transport chain (ETC) Mollusca respiratory complexes NADH:ubiquinone oxidoreductase cytochrome c oxidase |
spellingShingle |
Oceanography Marine Biology Marine Geoscience Biological Oceanography Chemical Oceanography Physical Oceanography Marine Engineering hypoxia reoxygenation post-translational modification (PTM) mitochondrial electron transport chain (ETC) Mollusca respiratory complexes NADH:ubiquinone oxidoreductase cytochrome c oxidase Halina I. Falfushynska Eugene Sokolov Helen Piontkivska Inna M. Sokolova Data_Sheet_7_The Role of Reversible Protein Phosphorylation in Regulation of the Mitochondrial Electron Transport System During Hypoxia and Reoxygenation Stress in Marine Bivalves.PDF |
topic_facet |
Oceanography Marine Biology Marine Geoscience Biological Oceanography Chemical Oceanography Physical Oceanography Marine Engineering hypoxia reoxygenation post-translational modification (PTM) mitochondrial electron transport chain (ETC) Mollusca respiratory complexes NADH:ubiquinone oxidoreductase cytochrome c oxidase |
description |
Fluctuations in the ambient oxygen concentrations represent a major stressor for aerobic organisms causing ATP deficiency during hypoxia and excessive production of reactive oxygen species during reoxygenation. Modulation of the mitochondrial electron transport system activity was proposed as a major mechanism involved in both the mitochondrial injury and adaptive response, but the mechanisms of ETS regulation during hypoxia/reoxygenation (H/R) stress remain poorly understood in hypoxia-tolerant organisms. To address this gap, we focused on the effects of H/R on activities of the mitochondrial Complexes I and IV in hypoxia-tolerant marine bivalves, the blue mussel Mytilus edulis, the Arctic quahog Arctica islandica and the Pacific oyster Crassostrea gigas, exposing them for 1 or 6 days to extreme hypoxia (<0.1% O 2 ) followed by 1 h of reoxygenation. We used a combination of bioinformatics analysis, biochemical and molecular studies to examine the potential role of the reversible protein phosphorylation in regulation of the Complex I and IV activities and in the mitochondrial responses to H/R stress. Our results showed a strong species-specific modulation of two important kinases, the serine/threonine protein kinase A (PKA) and protein kinase C (PKC) by H/R stress in the studied bivalves. The mitochondrial Complexes I and IV emerged as important targets for modulation by H/R stress, mediated in part through reversible phosphorylation by PKA and PKC. The effects of the reversible phosphorylation on the enzyme activities were species- and condition-specific. In mussels and quahogs, phosphorylation by PKA and PKC led to a strong increase in activity of Complexes I and IV. In oysters, Complexes I and IV were insensitive to PKA and PKC activation except after prolonged hypoxia and reoxygenation when elevated sensitivity to PKA and PKC activation indicated a change in the configuration and/or isoform composition of these enzymes. Non-site-specific dephosphorylation strongly suppressed the activity of Complex I and ... |
format |
Dataset |
author |
Halina I. Falfushynska Eugene Sokolov Helen Piontkivska Inna M. Sokolova |
author_facet |
Halina I. Falfushynska Eugene Sokolov Helen Piontkivska Inna M. Sokolova |
author_sort |
Halina I. Falfushynska |
title |
Data_Sheet_7_The Role of Reversible Protein Phosphorylation in Regulation of the Mitochondrial Electron Transport System During Hypoxia and Reoxygenation Stress in Marine Bivalves.PDF |
title_short |
Data_Sheet_7_The Role of Reversible Protein Phosphorylation in Regulation of the Mitochondrial Electron Transport System During Hypoxia and Reoxygenation Stress in Marine Bivalves.PDF |
title_full |
Data_Sheet_7_The Role of Reversible Protein Phosphorylation in Regulation of the Mitochondrial Electron Transport System During Hypoxia and Reoxygenation Stress in Marine Bivalves.PDF |
title_fullStr |
Data_Sheet_7_The Role of Reversible Protein Phosphorylation in Regulation of the Mitochondrial Electron Transport System During Hypoxia and Reoxygenation Stress in Marine Bivalves.PDF |
title_full_unstemmed |
Data_Sheet_7_The Role of Reversible Protein Phosphorylation in Regulation of the Mitochondrial Electron Transport System During Hypoxia and Reoxygenation Stress in Marine Bivalves.PDF |
title_sort |
data_sheet_7_the role of reversible protein phosphorylation in regulation of the mitochondrial electron transport system during hypoxia and reoxygenation stress in marine bivalves.pdf |
publishDate |
2020 |
url |
https://doi.org/10.3389/fmars.2020.00467.s007 https://figshare.com/articles/dataset/Data_Sheet_7_The_Role_of_Reversible_Protein_Phosphorylation_in_Regulation_of_the_Mitochondrial_Electron_Transport_System_During_Hypoxia_and_Reoxygenation_Stress_in_Marine_Bivalves_PDF/12598877 |
geographic |
Arctic Pacific |
geographic_facet |
Arctic Pacific |
genre |
Arctic Arctica islandica Crassostrea gigas Pacific oyster |
genre_facet |
Arctic Arctica islandica Crassostrea gigas Pacific oyster |
op_relation |
doi:10.3389/fmars.2020.00467.s007 https://figshare.com/articles/dataset/Data_Sheet_7_The_Role_of_Reversible_Protein_Phosphorylation_in_Regulation_of_the_Mitochondrial_Electron_Transport_System_During_Hypoxia_and_Reoxygenation_Stress_in_Marine_Bivalves_PDF/12598877 |
op_rights |
CC BY 4.0 |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.3389/fmars.2020.00467.s007 |
_version_ |
1766348824879562752 |