NDLI: Characterization of phytochelatin synthase produced by the primitive red alga Cyanidioschyzon merolae

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Characterization of phytochelatin synthase produced by the primitive red alga Cyanidioschyzon merolae

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Metallomics Vol - 1 Issue - 3

Metallomics Vol - 1 Issue - 2

Metallomics Vol - 1 Issue - 1

Characterization of phytochelatin synthase produced by the primitive red alga Cyanidioschyzon merolae

Content Provider	Royal Society of Chemistry (RSC)
Author	Wakagi, Takayoshi Osaki, Yuko Yoshimura, Etsuro Nakanishi, Hiromi Shirabe, Tomoo
Copyright Year	2009
Abstract	Phytochelatins (PCs), non-proteinpeptides with the general structure [(γ-Glu-Cys)n-Gly (n ≥ 2)], are involved in the detoxification of toxic heavy metals mainly in higher plants. The synthesis of the peptides is mediated by phytochelatin synthase (PCS), which is activated by a range of heavy metals. CmPCS, a PCS-like gene found in the genomic DNA of the primitive red alga Cyanidioschyzon merolae, was isolated and a recombinant protein (rCmPCS) fused with a hexahistidine tag at the N-terminus of CmPCS was produced. The finding that this protein mediated PC synthesis from glutathione in a metal-dependent way clearly establishes that rCmPCS is functional. The maximum activity was attained at a reaction temperature of 50 °C, considerably higher than the temperature required for the maximal activity of PCS isolated from the higher plant Silene cucubalus, probably due to the alga being a thermophile. CmPCS showed optimal pH in a slightly higher region than higher plant PCSs, probably due to the less effective charge relay network in the catalytic triad. In addition, the pattern of enzyme activation by metal ions was specific to rCmPCS, with Ag+, Cu2+, and Hg2+ showing only limited activation. In contrast to other eukaryotic PCSs, CmPCS has an extra domain in the N-terminal region from residues 1 to 109, and contains fewer cysteine residues in the C-terminal domain. These differences may be responsible for the metal specificity of the activation of CmPCS. Although the enzyme preparation lost PCS activity progressively when stored at 4 °C, the inclusion of Cd2+ in the preparation effectively prevented the reduction of activity. Furthermore, Cd2+ effectively restored the activity of the inactivated enzyme. These results indicate that Cd2+ ions bind the enzyme to maintain the structural integrity of the peptides.
Starting Page	353
Ending Page	358
Page Count	6
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	1
Issue Number	4
Journal	Metallomics
DOI	10.1039/b823013g
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Cysteine Personal computer Enzyme Algae Red algae Eukaryote Vascular plant Protein C-terminus Cyanidioschyzon merolae N-terminus Gene Catalytic triad Thermophile DNA Organosilicon PH Silene Glutathione
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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A Functional Putative Phytochelatin Synthase from the Primitive Red Alga Cyanidioschyzon merolae

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Characterization of phytochelatin synthase produced by the primitive red alga Cyanidioschyzon merolae

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