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Cell Stress Chaperones. 2018 Sep;23(5):933-941. doi: 10.1007/s12192-018-0900-7. Epub 2018 Apr 25.

Characterizing functional differences in sea anemone Hsp70 isoforms using budding yeast.

Author information

1
Department of Biological Sciences, University of North Carolina Charlotte, Charlotte, NC, 28223, USA.
2
Department of Biological Sciences, University of North Carolina Charlotte, Charlotte, NC, 28223, USA. atruman1@uncc.edu.

Abstract

Marine organisms experience abiotic stressors such as fluctuations in temperature, UV radiation, salinity, and oxygen concentration. Heat shock proteins (HSPs) assist in the response of cells to these stressors by refolding and maintaining the activity of damaged proteins. The well-conserved Hsp70 chaperone family is essential for cell viability as well as the response to stress. Organisms possess a variety of Hsp70 isoforms that differ slightly in amino acid sequence, yet very little is known about their functional relevance. In this study, we undertook analysis of three principal Hsp70 isoforms NvHsp70A, B, and D from the starlet sea anemone Nematostella vectensis. The functionality of Hsp70 isoforms in the starlet sea anemone was assessed through transcriptional analysis and by heterologous expression in budding yeast Saccharomyces cerevisiae. Interestingly, these isoforms were found to not only differ in expression under stress but also appear to have functional differences in their ability to mediate the cellular stress program. These results contribute to an understanding of Hsp70 isoform specificity, their shared and unique roles in response to acute and chronic environmental stress, and the potential basis of local adaptation in populations of N. vectensis.

KEYWORDS:

Hsp70; Isoform diversity; Molecular chaperone; Nematostella vectensis

PMID:
29696514
PMCID:
PMC6111083
DOI:
10.1007/s12192-018-0900-7
[Indexed for MEDLINE]
Free PMC Article

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