Edinburgh Research Explorer

Algal phospho- and protein rhythms mass spec data

Dataset

Related Edinburgh Organisations

PublisherEdinburgh DataVault
Date of data production2013 - 2014
Date made available2019

Description

Circadian protein regulation in the green lineage I.
A phospho-dawn anticipates light onset before proteins peak in daytime.

## Format ##
Thermo .raw mass spectrometer files. This file format can be opened using Thermo Fisher Scientific's Xcalibur software.

## Access ##
This dataset is held in the Edinburgh DataVault, directly accessible only to authorised University of Edinburgh users. External users may request access to a copy of the data by contacting the Principal Investigator, Contact Person or Data Manager named on this page. University of Edinburgh users who wish to have direct access should consult the information about retrieving data from the DataVault at: http://www.ed.ac.uk/is/research-support/datavault .

Abstract

Daily light-dark cycles (LD) drive dynamic regulation of plant and algal transcriptomes via photoreceptor pathways and 24-hour, circadian rhythms. Diel regulation of protein levels and modifications has been less studied. Ostreococcus tauri, the smallest free-living eukaryote, provides a minimal model proteome for the green lineage. Here, we compare transcriptome data under LD to the algal proteome and phosphoproteome, assayed using shotgun mass spectrometry. Under 10% of 855 quantified proteins were rhythmic but two-thirds of 860 phosphoproteins showed rhythmic modification(s). Most rhythmic proteins peaked in the daytime. Model simulations showed that light-stimulated protein synthesis largely accounts for this distribution of protein peaks. Prompted by apparently dark-stable proteins, we sampled during prolonged dark adaptation, where stable RNAs and very limited change to the proteome suggested a quiescent, cellular “dark state”. In LD, acid-directed and proline directed protein phosphorylation sites were regulated in antiphase. Strikingly, 39% of rhythmic phospho-sites reached peak levels just before dawn. This anticipatory phosphorylation is distinct from light-responsive translation but consistent with plant phosphoprotein profiles, suggesting that a clock-regulated phospho-dawn prepares green cells for daytime functions.

Data Citation

Millar A et al. "Algal phospho- and protein rhythms" [dataset] University of Edinburgh

Contact person

Reason for data restriction and conditions for release

This dataset is held in the Edinburgh DataVault, directly accessible only to authorised University of Edinburgh users. External users may request access to a copy of the data by contacting the Depositor, or in their absence the Contact Person or Data Manager named on this page. Further information on retrieving data from the DataVault can be found at: "http://www.ed.ac.uk/is/research-support/datavault

Physical data

  • Algal phospho- and protein rhythms mass spec data

    Storage locationEdinburgh DataVault
    Access descriptionThis dataset is held in the DataVault, directly accessible only to authorised University of Edinburgh staff. To request a copy, contact the Depositor, or the Contact Person or Data Manager. Further info: http://www.ed.ac.uk/is/research-support/datavault
    Mediahttps://www.ed.ac.uk/is/research-support/datavault
    TypeDataset

ID: 82482794