Characterization of Peptidyl-Prolyl Cis-Trans Isomerase- and Calmodulin-Binding Activity of a Cytosolic Arabidopsis thaliana Cyclophilin AtCyp19-3
Identifieur interne : 001C90 ( Ncbi/Curation ); précédent : 001C89; suivant : 001C91Characterization of Peptidyl-Prolyl Cis-Trans Isomerase- and Calmodulin-Binding Activity of a Cytosolic Arabidopsis thaliana Cyclophilin AtCyp19-3
Auteurs : Gundeep Kaur [Inde] ; Supreet Singh [Inde] ; Harpreet Singh [Inde] ; Mrinalini Chawla [Inde] ; Tanima Dutta [Inde] ; Harsimran Kaur [Inde] ; Kyle Bender [Canada] ; W. A. Snedden [Canada] ; Sanjay Kapoor [Inde] ; Ashwani Pareek [Inde] ; Prabhjeet Singh [Inde]Source :
- PLoS ONE [ 1932-6203 ] ; 2015.
Abstract
Cyclophilins, which bind to immunosuppressant cyclosporin A (CsA), are ubiquitous proteins and constitute a multigene family in higher organisms. Several members of this family are reported to catalyze
Url:
DOI: 10.1371/journal.pone.0136692
PubMed: 26317213
PubMed Central: 4552658
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Isomerase- and Calmodulin-Binding Activity of a Cytosolic <italic>Arabidopsis thaliana</italic>
Cyclophilin AtCyp19-3</title>
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Isomerase- and Calmodulin-Binding Activity of a Cytosolic <italic>Arabidopsis thaliana</italic>
Cyclophilin AtCyp19-3</title>
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<front><div type="abstract" xml:lang="en"><p>Cyclophilins, which bind to immunosuppressant cyclosporin A (CsA), are ubiquitous proteins and constitute a multigene family in higher organisms. Several members of this family are reported to catalyze <italic>cis-trans</italic>
isomerisation of the peptidyl-prolyl bond, which is a rate limiting step in protein folding. The physiological role of these proteins in plants, with few exceptions, is still a matter of speculation. Although <italic>Arabidopsis</italic>
genome is predicted to contain 35 cyclophilin genes, biochemical characterization, imperative for understanding their cellular function(s), has been carried only for few of the members. The present study reports the biochemical characterization of an <italic>Arabidopsis</italic>
cyclophilin, AtCyp19-3, which demonstrated that this protein is enzymatically active and possesses peptidyl-prolyl <italic>cis-trans</italic>
isomerase (PPIase) activity that is specifically inhibited by CsA with an inhibition constant (K<sub>i</sub>
) of 18.75 nM. The PPIase activity of AtCyp19-3 was also sensitive to Cu<sup>2+</sup>
, which covalently reacts with the sulfhydryl groups, implying redox regulation. Further, using calmodulin (CaM) gel overlay assays it was demonstrated that <italic>in vitro</italic>
interaction of AtCyp19-3 with CaM is Ca<sup>2+</sup>
-dependent, and CaM-binding domain is localized to 35–70 amino acid residues in the N-terminus. Bimolecular fluorescence complementation assays showed that AtCyp19-3 interacts with CaM <italic>in vivo</italic>
also, thus, validating the <italic>in vitro</italic>
observations. However, the PPIase activity of the <italic>Arabidopsis</italic>
cyclophilin was not affected by CaM. The implications of these findings are discussed in the context of Ca<sup>2+</sup>
signaling and cyclophilin activity in <italic>Arabidopsis</italic>
.</p>
</div>
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