Glutathione S-Transferase (GST) Gene Diversity in the Crustacean Calanus finmarchicus--Contributors to Cellular Detoxification

PLoS One. 2015 May 6;10(5):e0123322. doi: 10.1371/journal.pone.0123322. eCollection 2015.

Abstract

Detoxification is a fundamental cellular stress defense mechanism, which allows an organism to survive or even thrive in the presence of environmental toxins and/or pollutants. The glutathione S-transferase (GST) superfamily is a set of enzymes involved in the detoxification process. This highly diverse protein superfamily is characterized by multiple gene duplications, with over 40 GST genes reported in some insects. However, less is known about the GST superfamily in marine organisms, including crustaceans. The availability of two de novo transcriptomes for the copepod, Calanus finmarchicus, provided an opportunity for an in depth study of the GST superfamily in a marine crustacean. The transcriptomes were searched for putative GST-encoding transcripts using known GST proteins from three arthropods as queries. The identified transcripts were then translated into proteins, analyzed for structural domains, and annotated using reciprocal BLAST analysis. Mining the two transcriptomes yielded a total of 41 predicted GST proteins belonging to the cytosolic, mitochondrial or microsomal classes. Phylogenetic analysis of the cytosolic GSTs validated their annotation into six different subclasses. The predicted proteins are likely to represent the products of distinct genes, suggesting that the diversity of GSTs in C. finmarchicus exceeds or rivals that described for insects. Analysis of relative gene expression in different developmental stages indicated low levels of GST expression in embryos, and relatively high expression in late copepodites and adult females for several cytosolic GSTs. A diverse diet and complex life history are factors that might be driving the multiplicity of GSTs in C. finmarchicus, as this copepod is commonly exposed to a variety of natural toxins. Hence, diversity in detoxification pathway proteins may well be key to their survival.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthropod Proteins / chemistry
  • Arthropod Proteins / genetics*
  • Arthropod Proteins / metabolism
  • Crustacea / enzymology
  • Crustacea / genetics*
  • Cytoplasm / enzymology
  • Genetic Variation*
  • Glutathione Transferase / chemistry
  • Glutathione Transferase / genetics*
  • Glutathione Transferase / metabolism
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Microsomes / enzymology
  • Mitochondria / enzymology
  • Molecular Sequence Data
  • Phylogeny
  • Transcriptome

Substances

  • Arthropod Proteins
  • Isoenzymes
  • Glutathione Transferase

Associated data

  • BioProject/PRJNA236528

Grants and funding

This research is based upon work supported by the National Science Foundation under grants OCE-1040597 to PHL, IOS-1353023 to AEC and ABI-1062432 to Indiana University, as well as by the Cades Foundation of Honolulu, Hawaii. VR acknowledges the Mount Desert Island Biological Laboratory’s David W. Towle Fellowship for Graduate Student Research for supporting her Summer 2012 field work conducted at the Mount Desert Island Biological Laboratory (Bar Harbor, Maine). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.