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The catalytic domain CysPc of the DEK 1 calpain is functionally conserved in land plants
Author(s) -
Liang Zhe,
Demko Viktor,
Wilson Robert C.,
Johnson Kenneth A.,
Ahmad Rafi,
Perroud PierreFrançois,
Quatrano Ralph,
Zhao Sen,
ShalchianTabrizi Kamran,
Otegui Marisa S.,
Olsen OddArne,
Johansen Wenche
Publication year - 2013
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.12235
Subject(s) - complementation , mutant , arabidopsis thaliana , biology , calpain , protein fragment complementation assay , phylogenetic tree , genetics , gene , phylogenetics , bimolecular fluorescence complementation , biochemistry , enzyme
Summary DEK 1, the single calpain of land plants, is a member of the ancient membrane bound TML –CysPc–C2L calpain family that dates back 1.5 billion years. Here we show that the CysPc–C2L domains of land plant calpains form a separate sub‐clade in the DEK 1 clade of the phylogenetic tree of plants. The charophycean alga M esostigma viride DEK 1 ‐like gene is clearly divergent from those in land plants, suggesting that a major evolutionary shift in DEK 1 occurred during the transition to land plants. Based on genetic complementation of the A rabidopsis thaliana dek1‐3 mutant using CysPc–C2L domains of various origins, we show that these two domains have been functionally conserved within land plants for at least 450 million years. This conclusion is based on the observation that the CysPc–C2L domains of DEK 1 from the moss P hyscomitrella patens complements the A. thaliana dek1‐3 mutant phenotype. In contrast, neither the CysPc–C2L domains from M. viride nor chimeric animal–plant calpains complement this mutant. Co‐evolution analysis identified differences in the interactions between the CysPc–C2L residues of DEK 1 and classical calpains, supporting the view that the two enzymes are regulated by fundamentally different mechanisms. Using the A. thaliana dek1‐3 complementation assay, we show that four conserved amino acid residues of two Ca 2+ ‐binding sites in the CysPc domain of classical calpains are conserved in land plants and functionally essential in A. thaliana DEK 1.