Disentangling thermal stress responses in a reef-calcifier and its photosymbionts by shotgun proteomics

peer-reviewed · Scientific Reports · 2018

peer-reviewed · Scientific Reports · 2018. Marleen Stuhr et al. The proliferation of key marine ecological engineers and carbonate producers often relies on their…
Date 2018-02-23
Type peer-reviewed
Venue Scientific Reports
Publisher Springer Science and Business Media LLC
Contribution downstream-application
DOI 10.1038/s41598-018-21875-z
Citations (OpenAlex) 34
Venue 2-year citedness 5.08

Abstract

The proliferation of key marine ecological engineers and carbonate producers often relies on their association with photosymbiotic algae. Evaluating stress responses of these organisms is important to predict their fate under future climate projections. Physiological approaches are limited in their ability to resolve the involved molecular mechanisms and attribute stress effects to the host or symbiont, while probing and partitioning of proteins cannot be applied in organisms where the host and symbiont are small and cannot be physically separated. Here we apply a label-free quantitative proteomics approach to detect changes of proteome composition in the diatom-bearing benthic foraminifera Amphistegina gibbosa experimentally exposed to three thermal-stress scenarios. We developed a workflow for protein extraction from less than ten specimens and simultaneously analysed host and symbiont proteomes. Despite little genomic data for the host, 1,618 proteins could be partially assembled and assigned. The proteomes revealed identical pattern of stress response among stress scenarios as that indicated by physiological measurements, but allowed identification of compartment-specific stress reactions. In the symbiont, stress-response and proteolysis-related proteins were up regulated while photosynthesis-related proteins declined. In contrast, host homeostasis was maintained through chaperone up-regulation associated with elevated proteosynthesis and proteolysis, and the host metabolism shifted to heterotrophy.

Authors

  1. Marleen Stuhr · Leibniz Centre for Tropical Marine Research
  2. Bernhard Blank-Landeshammer · Leibniz Institute for Analytical Sciences - ISAS, Leibniz-Institut für Analytische Wissenschaften (ISAS)
  3. Claire E. Reymond · Leibniz Centre for Tropical Marine Research
  4. Laxmikanth Kollipara · Leibniz Institute for Analytical Sciences - ISAS, Leibniz-Institut für Analytische Wissenschaften (ISAS)
  5. Albert Sickmann · Leibniz Institute for Analytical Sciences - ISAS, Leibniz-Institut für Analytische Wissenschaften (ISAS), Ruhr University Bochum, University of Aberdeen
  6. Michal Kucera · University of Bremen
  7. Hildegard Westphal · Leibniz Centre for Tropical Marine Research, University of Bremen

Methods and tools

Methods it uses

  • PEAKS: Commercial DP-based de novo
  • SPIDER: Protein identification from sequence tags while accounting for de novo sequencing error.

Data deposited

  • Dual-compartment shotgun proteomics unravel thermal stress responses in reef-calcifiers and their photosymbionts — as deposited · PXD008015

Cites (3)

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