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Cysteine-rich peptides (CRPs), disulfide-constrained peptides with three to five disulfide bonds and molecular weights of 2 to 6 kDa, are generally hyperstable and resistant to thermal, chemical and enzymatic degradation. Here, the discovery and characterization of a novel suite of CRPs, collectively named potentides pA1- pA16 from the root of the medicinal herb Potentilla anserina L, are described. Using a combination of proteomic and transcriptomic methods, we showed that 35-residue potentide pA3, the most abundant member of potentides, exhibits high stability against heat, acidic and proteolytic degradation. Transcriptomic analysis revealed that potentide precursor sequences contain four tandem repeats for mature domain, which is the first report that the tandem repeats are found in the Rosaceae family. Disulfide mapping showed that potentide pA3 displays a novel disulfide connectivity of C1-C3, C2-C6 and C4-C5, a cystine motif that has not been reported in plant CRPs. Transcriptomic data mining and a neighbor-joining clustering analysis revealed 56 potentide homologs and their distribution in the families of Rosaceae and Ranunculaceae in angiosperm. Altogether, these results reveal a new plant CRP structure with an unusual cystine connectivity. Additionally, this study expands the families and structure diversity of CRPs as potentially active peptide pharmaceuticals.
This article was published in the following journal.
Name: Chembiochem : a European journal of chemical biology
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A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.
A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
A subfamily of ligand-gated ion channel receptors that share a characteristic loop which is formed by a disulfide bond between two CYSTEINE residues. These receptors typically contain five subunits with the cysteine-loop occurring near an N-terminal extracellular domain.
A structurally-related family of small proteins that form a stable tertiary fold pattern which is supported by a series of disulfide bonds. The arrangement of disulfide bonds between the CYSTEINE moieties results in a knotted structure which is unique to this family of proteins.
A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.
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