The proteomic response of sea squirts (genus Ciona ) to acute heat stress: A global perspective on the thermal stability of proteins

• Published in: Comparative Biochemistry and Physiology Part D: Genomics and Proteomics
• Main Authors: Serafini, Loredana, Hann, Jay B., Kültz, Dietmar, Tomanek, Lars
• Format: Text
• Language: unknown
• Published: DigitalCommons@CalPoly 2011
• Subjects: Ciona; Cytoskeleton; Heat stress; Molecular chaperones; Proteomics; Biology; Arctic; Pacific
• Online Access: https://digitalcommons.calpoly.edu/bio_fac/379; https://doi.org/10.1016/j.cbd.2011.07.002; https://digitalcommons.calpoly.edu/context/bio_fac/article/1386/viewcontent/TomanekL_2011_TheProteomicResponseSeaSquirts.pdf

Congeners belonging to the genus Ciona have disparate distributions limited by temperature. Ciona intestinalis is more widespread with a cosmopolitan distribution ranging from tropical to sub-arctic zones, while Ciona savignyi is limited to temperate-latitudes of the northern Pacific Ocean. To compare the heat stress response between congeners, we quantified changes in protein expression using proteomics. Animals were exposed to 22 °C, 25 °C, and 28 °C for 6 h, then recovered at a control temperature (13 °C) for 16 h (high heat stress experiment). In a second experiment we exposed animals to lower levels of heat stress at 18 °C, 20 °C, and 23 °C, with a 16 °C control. A quantitative analysis, using 2D gel electrophoresis and MALDI-TOF/TOF mass spectrometry (with a 69% and 93% identification rate for Ciona intestinalis and Ciona savignyi, respectively), showed changes in a number of protein functional groups, including molecular chaperones, extracellular matrix proteins, calcium-binding proteins, cytoskeletal proteins and proteins involved in energy metabolism. Our results indicate that C. intestinalis maintains higher constitutive levels of molecular chaperones than C. savignyi, suggesting that it is prepared to respond faster to thermal stress. Systematic discrepancies between estimated versus predicted molecular masses of identified proteins differed between protein families and were more pronounced under high heat conditions, suggesting that thermal sensitivities are lower for cytoskeletal proteins and ATPsynthase than for any other protein group represented on 2D gels.