Abstract
In their role as molecular chaperones, heat shock proteins (Hsps) mediate protein folding thereby mitigating cellular damage caused by physiological and environmental stress. Nauplii of the crustacean Artemia franciscana respond to heat shock by producing Hsps; however, the effects of cold shock on Hsp levels in A. franciscana have not been investigated previously. The effect of cold shock at 1 °C followed by recovery at 27 °C on the amounts of ArHsp90, Hsp70, ArHsp40, and ArHsp40-2 mRNA and their respective proteins in A. franciscana nauplii was examined by quantitative PCR (qPCR) and immunoprobing of western blots. The same Hsp mRNAs and proteins were also quantified during incubation of nauplii at their optimal growth temperature of 27 °C. qPCR analyses indicated that the abundance of ArHsp90, Hsp70, and ArHsp40 mRNA remained relatively constant during both cold shock and recovery and was not significantly different compared with levels at optimal temperature. Western blotting revealed that ArHsp90, ArHsp40, and ArHsp40-2 were generally below baseline, but at detectable levels during the 6 h of cold shock, and persisted in early recovery stages before declining. Hsp70 was the only protein that remained constant in quantity throughout cold shock and recovery. By contrast, all Hsps declined rapidly during 6 h when nauplii were incubated continuously at 27 °C optimal temperature. Generally, the amounts of ArHsp90, ArHsp40, and ArHsp40-2 were higher during cold shock/recovery than those during continuous incubation at 27 °C. Our data support the conclusion that low temperature preserves Hsp levels, making them available to assist in protein repair and recovery after cold shock.
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Data availability
All data for Hsp mRNA and protein are available in Microsoft Excel files, version 16.35 (Microsoft 2020).
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Acknowledgments
We thank Jiabo Tan, Andrew Schofield, Sheethal Panchakshari, and two anonymous reviewers for their advice and contributions to this work.
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All codes are available for data analyzed with RStudio, an adjacent platform of the statistical software, R, version 3.6.0 (R Core Team 2018).
Funding
This project was funded by the Natural Sciences and Engineering Research Council of Canada (NSERC) Discovery Grant (Number RGPIN/04882-2016) to THM and a scholarship from Imhotep’s Legacy Academy at Dalhousie University to YAG.
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All authors contributed to the study conception and design. Material preparation and data collection were performed by YAG. Data analyses were performed by YAG and LKW. The first draft of the manuscript was written by YAG, THM, and LKW and all authors commented on previous versions and reviews of the manuscript. All authors have read and approved the final manuscript.
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This research was performed in accordance with the ethical guidelines provided by the Canadian Council on Animal Care (CCAC). The University Committee on Laboratory Animals (UCLA) of Dalhousie University approved the research under assigned Protocol Number 117-36.
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Online Resource 1
Stained gels and blots containing proteins from A. franciscana nauplii. Gels were stained with Colloidal Coomassie Brilliant Blue to demonstrate equal protein loading in each lane (a, b) and blots were stained with Ponceau to confirm successful protein transfer (c, d). Faint staining at the upper right, especially in the cold shock/recovery gel and blot, indicates minor degradation of proteins in late instar II nauplii (PDF 2568 kb)
Online Resource 2
Full western blots of Hsps in A. franciscana nauplii. ArHsp90, Hsp70, ArHsp40, and ArHsp40-2 were detected after immunoprobing with antibodies during a, continuous incubation at 27 °C and b, cold shock/recovery at 1 °C followed by incubation at 27 °C. Protein bands detected at the bottom of some blots represent possible minimal degradation (PDF 370 kb)
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Gbotsyo, Y.A., Rowarth, N.M., Weir, L.K. et al. Short-term cold stress and heat shock proteins in the crustacean Artemia franciscana. Cell Stress and Chaperones 25, 1083–1097 (2020). https://doi.org/10.1007/s12192-020-01147-4
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DOI: https://doi.org/10.1007/s12192-020-01147-4