Periaxin is expressed in mammalian Schwann cells and lens fiber cells, and has been identified in a screen for cytoskeleton-associated proteins. Charcot-Marie-Tooth 4F is caused by losses or mutations of the periaxin gene. The periaxin gene encodes two protein isoforms, namely, L-periaxin and S-periaxin. S-periaxin contains 147 amino acid residues and has an N-terminal PDZ domain. In this paper, S-periaxin was reported to be homodimerized through the formation of intermolecular disulfide bonds with its Cys88 and Cys139 residues under mild oxidation conditions. The covalent dimer of S-periaxin was also observed by western blot analysis and bimolecular fluorescence complementation analyses. S-periaxin dimerization formation could be regulated by cellular redox fluctuations. These results offer a possible mechanism to the formation of periaxin complexes, improvement of complex stability, and establishment of a link between the extracellular matrix and the cytoskeleton.
A novel antifungal protein was isolated from naked oat (Avena nuda) seeds by acetone fractionation, (NH4)2SO4 precipitation, Q‐Sepharose ion‐exchange chromatography, chitin affinity chromatography, and Sephacryl S‐200 gel filtration chromatography. The antifungal protein exhibited a molecular mass of 23,760, as measured by gel filtration and SDS‐PAGE. Matrix‐assisted laser desorption ionization–time of flight MS analysis indicated that the protein was homologous with a permatin precursor from A. sativa. The protein from naked oats exhibited antifungal activity against Trametes sp. SQ01 (half‐maximal inhibitory concentration [IC50] = 5.68μM), Trichoderma spp. (IC50 = 0.83μM), and Chaetomium sp. R01.
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