Data from: Differential proteomic responses of selectively bred and wild Sydney rock oyster populations exposed to elevated CO2

Previous work suggests that larvae from Sydney rock oysters that have been selectively bred for fast growth and disease resistance are more resilient to the impacts of ocean acidification than nonselected, wild-type oysters. In this study, we used proteomics to investigate the molecular differences between oyster populations in adult Sydney rock oysters and to identify whether these form the basis for observations seen in larvae. Adult oysters from a selective breeding line (B2) and nonselected wild types (WT) were exposed for 4 weeks to elevated pCO2 (856 μatm) before their proteomes were compared to those of oysters held under ambient conditions (375 μatm pCO2). Exposure to elevated pCO2 resulted in substantial changes in the proteomes of oysters from both the selectively bred and wild-type populations. When biological functions were assigned, these differential proteins fell into five broad, potentially interrelated categories of subcellular functions, in both oyster populations. These functional categories were energy production, cellular stress responses, the cytoskeleton, protein synthesis and cell signalling. In the wild-type population, proteins were predominantly upregulated. However, unexpectedly, these cellular systems were downregulated in the selectively bred oyster population, indicating cellular dysfunction. We argue that this reflects a trade-off, whereby an adaptive capacity for enhanced mitochondrial energy production in the selectively bred population may help to protect larvae from the effects of elevated CO2, whilst being deleterious to adult oysters.

Usage Notes

Raw mass spec files from differentially expressed proteins of Sydney rock oysters - spot 211Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 211.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 213Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 213.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 214Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 214.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 306Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 306.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 308Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 308.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 502Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 502.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 1007Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 1007.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 1404Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 1404.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 1405Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 1405.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 1406Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 1406.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 1407Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 1407.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 1607Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 1607.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 1705Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 1705.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 1706Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 1706.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 1807Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 1807.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 2306Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 2306.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 2707Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 2707.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 2804Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 2804.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 3110Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mass spectrometer (Thermo scientific, CA, USA). Samples represent differentially expressed proteins from two populations of Sydney rock oyster at ambient and elevated CO2 exposure.ET121113_spot 3110.rawRaw mass spec files from differentially expressed proteins of Sydney rock oysters_spot 3304Tryptic peptides were analysed by reversed phase nanoflow liquid chromatography-tandem mass spectrometry (LC-MS/MS) on an QExactive mas....see Dryad link for full text