Meeting Abstract
Heat shock protein 70 (Hsp70) is a nearly universal class of molecular chaperones that are involved in diverse molecular pathways through specific interactions with other proteins. Most organisms have numerous Hsp70s encoded in their genome but it is not understood how similar the client proteins are for these Hsp70 homologs in ambient or heat stress conditions. Here we provide the first description of the homolog-specific diversity of Hsp70 clients for a marine invertebrate species, the cnidarian Nematostella vectensis, through heterologous expression in yeast. Using mass spectrometry we determined that three Hsp70s from this sea anemone interact with 100s of proteins. Despite the high sequence similarity of the Hsp70s, less than 50% of identified interacting proteins were common to all three anemone Hsp70s and as many as 18% were unique to an individual Hsp70. The overall enrichment of functions for these interacting proteins was similar for each Hsp70 despite this limited conservation of particular client proteins. Our study provides the first data set defining the potential “interactome” of Hsp70s for a marine species and suggest numerous specific interactions for Hsp70 homologs. Together, these data reveal a rich set of interacting proteins for Hsp70 that may be novel biomarkers to characterize the response of cnidarians to their rapidly changing environments.
