Phylogenetic characterization and promoter expression analysis of a novel hybrid protein disulfide isomerase/cargo receptor subfamily unique to plants and chromalveolates

Protein disulfide isomerases (PDIs) play critical roles in protein folding by catalyzing the formation and rearrangement of disulfide bonds in nascent secretory proteins. There are six distinct PDI subfamilies in terrestrial plants. A unique feature of PDI-C subfamily members is their homology to th...

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Bibliographic Details
Published in:Molecular genetics and genomics : MGG 2016-02, Vol.291 (1), p.455-469
Main Authors: Yuen, Christen Y. L., Wong, Katharine, Christopher, David A.
Format: Article
Language:English
Subjects:
Animal Genetics and Genomics
Animals
Arabidopsis
Arabidopsis - genetics
Biochemistry
Biomedical and Life Sciences
Catalytic Domain - genetics
Endoplasmic reticulum
Endoplasmic Reticulum - genetics
Exons - genetics
Genes
Genomics
Glucuronidase - genetics
Golgi Apparatus - genetics
Human Genetics
Life Sciences
Microbial Genetics and Genomics
Original
Original Article
Phylogenetics
Phylogeny
Plant Genetics and Genomics
Promoter Regions, Genetic - genetics
Protein Disulfide-Isomerases - genetics
Protein Folding
Protein Structure, Tertiary
Stramenopiles
Thioredoxins - genetics
Yeast
Yeasts - genetics
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Summary:Protein disulfide isomerases (PDIs) play critical roles in protein folding by catalyzing the formation and rearrangement of disulfide bonds in nascent secretory proteins. There are six distinct PDI subfamilies in terrestrial plants. A unique feature of PDI-C subfamily members is their homology to the yeast retrograde (Golgi-to-endoplasmic reticulum) cargo receptor proteins, Erv41p and Erv46p. Here, we demonstrate that plant Erv41p/Erv46p-like proteins are divided into three subfamilies: ERV-A, ERV-B and PDI-C, which all possess the N-proximal and C-proximal conserved domains of yeast Erv41p and Erv46p. However, in PDI-C isoforms, these domains are separated by a thioredoxin domain. The distribution of PDI-C isoforms among eukaryotes indicates that the PDI-C subfamily likely arose through an ancient exon-shuffling event that occurred before the divergence of plants from stramenopiles and rhizarians. Arabidopsis has three PDI-C genes: PDI7, PDI12, and PDI13. PDI12- and PDI13-promoter: β-glucuronidase (GUS) gene fusions are co-expressed in pollen and stipules, while PDI7 is distinctly expressed in the style, hydathodes, and leaf vasculature. The PDI-C thioredoxin domain active site motif CxxS is evolutionarily conserved among land plants. Whereas PDI12 and PDI13 retain the CxxS motif, PDI7 has a CxxC motif similar to classical PDIs. We hypothesize that PDI12 and PDI13 maintain the ancestral roles of PDI-C in Arabidopsis, while PDI7 has undergone neofunctionalization. The unusual PDI/cargo receptor hybrid arrangement in PDI-C isoforms has no counterpart in animals or yeast, and predicts the need for pairing redox functions with cargo receptor processes during protein trafficking in plants and other PDI-C containing organisms.
ISSN:1617-4615
1617-4623
DOI:10.1007/s00438-015-1106-7