Abstract

Environmental metal pollution is a growing health risk to flora and fauna. It is therefore important to fully elucidate metal detoxification pathways. Phytochelatin synthase (PCS), an enzyme involved in the biosynthesis of phytochelatins (PCs), plays an important role in cadmium detoxification. The PCS and PCs are however not restricted to plants, but are also present in some lower metazoans. The model nematode Caenorhabditis elegans, for example, contains a fully functional phytochelatin synthase and phytochelatin pathway. By means of a transgenic nematode strain expressing a pcs-1 promoter-tagged GFP (pcs-1::GFP) and a pcs-1 specific qPCR assay, further evidence is presented that the expression of the C. elegans phytochelatin synthase gene (pcs-1) is transcriptionally non-responsive to a chronic (48 h) insult of high levels of zinc (500 μM) or acute (3 h) exposures to high levels of cadmium (300 μM). However, the accumulation of cadmium, but not zinc, is dependent on the pcs-1 status of the nematode. Synchrotron based X-ray fluorescence imaging uncovered that the cadmium body burden increased significantly in the pcs-1(tm1748) knockout allele. Taken together, this suggests that whilst the transcription of pcs-1 may not be mediated by an exposure zinc or cadmium, it is nevertheless an integral part of the cadmium detoxification pathway in C. elegans.

Highlights

  • Phytochelatin (PC), a non-ribosomal heavy-metal complexing peptide, was first identified in monocot and dicot plants [1]

  • By means of a transgenic nematode strain expressing a pcs-1 promoter-tagged GFP and a pcs-1 specific Quantitative PCR (qPCR) assay, further evidence is presented that the expression of the C. elegans phytochelatin synthase gene is transcriptionally non-responsive to a chronic (48 h) insult of high levels of zinc (500 μM) or acute (3 h) exposures to high levels of cadmium (300 μM)

  • The difference in chronic and acute exposure conditions were due to the different toxicities of the respective metals and the need to apply the same exposure conditions to all experimental platforms

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Summary

Introduction

Phytochelatin (PC), a non-ribosomal heavy-metal complexing peptide, was first identified in monocot and dicot plants [1]. They are characterized by a repetitive (γ-GluCys)nGly motif (where n typically ranges from 2 to 5) and their ability to bind to cadmium and other non-essential metals (e.g., arsenic and mercury) and essential heavy metals (such as copper and zinc) via cysteine thiol residues [1]. The N-terminal is more conserved than the C-terminal. It has been suggest that the N-terminal is may be linked to the activity of the enzyme and the C-terminal might be important for the regulation of the enzyme but not for the activity [3]

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