The proteomic response of the mussel congeners Mytilus galloprovincialis and M. trossulus to acute heat stress: implications for thermal tolerance limits and metabolic costs of thermal stress.
The Mediterranean blue mussel, Mytilus galloprovincialis, an invasive species in California, has displaced the more heat-sensitive native congener, Mytilus trossulus, from its former southern range, possibly due to climate change. By comparing the response of their proteomes to acute heat stress we sought to identify responses common to both species as well as differences that account for greater heat tolerance in the invasive. Mussels were acclimated to 13°C for four weeks and exposed to acute heat stress (24°C, 28°C and 32°C) for 1 h and returned to 13°C to recover for 24 h. Using two-dimensional gel electrophoresis and tandem mass spectrometry we identified 47 and 61 distinct proteins that changed abundance in M. galloprovincialis and M. trossulus, respectively. The onset temperatures of greater abundance of some members of the heat shock protein (Hsp) 70 and small Hsp families were lower in M. trossulus. The abundance of proteasome subunits was lower in M. galloprovincialis but greater in M. trossulus in response to heat. Levels of several NADH-metabolizing proteins, possibly linked to the generation of reactive oxygen species (ROS), were lower at 32°C in the cold-adapted M. trossulus whereas proteins generating NADPH, important in ROS defense, were higher in both species. The abundance of oxidative stress proteins was lower at 32°C in M. trossulus only, indicating that its ability to combat heat-induced oxidative stress is limited to lower temperatures. Levels of NAD-dependent deacetylase (sirtuin 5), which are correlated with lifespan, were lower in M. trossulus in response to heat stress. In summary, the expression patterns of proteins involved in molecular chaperoning, proteolysis, energy metabolism, oxidative damage, cytoskeleton and deacetylation revealed a common loci of heat stress in both mussels but also showed a lower sensitivity to high-temperature damage in the warm-adapted M. galloprovincialis, which is consistent with its expanding range in warmer waters.
Tomanek
Lars
L
California Polytechnic State University, Department of Biological Sciences, Center for Coastal Marine Sciences, Environmental Proteomics Laboratory, 1 Grand Avenue, San Luis Obispo, CA 93407-0401, USA. ltomanek@calpoly.edu
Zuzow
Marcus J
MJ
D000222:Adaptation, Physiological; D000332:Aerobiosis; D000693:Anaerobiosis; D000818:Animals; D016000:Cluster Analysis; D015180:Electrophoresis, Gel, Two-Dimensional; D004734:Energy Metabolism; D018869:Heat-Shock Response; D008954:Models, Biological; D049878:Mytilus / Q000378:metabolism*; D018384:Oxidative Stress; D010427:Pentose Phosphate Pathway; D025341:Principal Component Analysis; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000378:metabolism; D040901:Proteomics; D015398:Signal Transduction; D013045:Species Specificity; D013696:Temperature
D020543:Proteome