The evolution of heat shock protein 70 in sea anemones
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Date
2015-05
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The Ohio State University
Abstract
Heat shock protein 70 (Hsp70) is a ubiquitous protein that functions as a molecular
chaperone to repair damaged proteins. Found in all organisms from archaebacteria to humans,
Hsp70 is important in the response of organisms to a variety of environmental stressors such as
elevated temperature and oxidation. As the environmental conditions of our oceans are subjected
to the impacts of climate change, understanding the stress response of marine organisms is
becoming increasingly important to predict how marine organisms may respond to
environmental stressors. Cnidarians, including sea anemones and reef building corals, are
extremely important marine species which are susceptible to environmental stressors brought on
by climate change. To better understand the potential stress responses of these cnidarians,
characterizing Hsp70 diversity is necessary. To study how this gene has evolved, RNA was
extracted from 20 species of sea anemones and partial transcriptomes were sequenced.
Bioinformatic methods were then used to identify and extract candidate Hsp70 sequences from
each transcriptome. The extracted sequences for each species were then aligned and used to
create a tree of Hsp70 gene families. Across the focal taxa we observed variation in sequence
copy number and amino acid composition. Although variation in copy number was coupled with
the quality of the assembly, there was apparent concerted /birth-death gene family evolution
observed in the Hsp70 genes. Additionally, Hsp70 was highly conserved throughout the tree
indicating potential functional constraints or retained phylogenetic signal. The Hsp70 is just one
of many genes that can play a key role in a species resilience against climate change. Our
findings contribute to understanding the repertoire of genomic resilience across these species of
sea anemones.
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Keywords
evolution, environmental stress, marine ecology, hsp70