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Mo-CBP3, a 2S albumin from Moringa oleifera, is a complex mixture of isoforms that arise from different post-translational modifications

Mo-CBP3 is a chitin-binding 2S albumin from Moringa oleifera. This seed storage protein is resistant to thermal denaturation and shows biological activities that might be of practical use, such as antifungal properties against Candida sp., a pathogen that causes candidiasis, and against Fusarium sol...

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Published in:Plant physiology and biochemistry 2019-07, Vol.140, p.68-77
Main Authors: Freire, José E.C., Moreno, Frederico B.M.B., Monteiro-Júnior, José E., Sousa, Antônio J.S., Vasconcelos, Ilka M., Oliveira, José T.A., Monteiro-Moreira, Ana C.O., Rocha, Bruno A.M., Grangeiro, Thalles B.
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Language:English
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Summary:Mo-CBP3 is a chitin-binding 2S albumin from Moringa oleifera. This seed storage protein is resistant to thermal denaturation and shows biological activities that might be of practical use, such as antifungal properties against Candida sp., a pathogen that causes candidiasis, and against Fusarium solani, a soil fungus that can cause diseases in plants and humans. Previous work has demonstrated that Mo-CBP3 is a mixture of isoforms encoded by members of a small multigene family. Mature Mo-CBP3 is a small protein (∼14 kDa), constituted by a small chain of approximately 4 kDa and a large chain of 8 kDa, which are held together by disulfide bridges. However, a more comprehensive picture on the spectrum of Mo-CBP3 isoforms which are found in mature seeds, is still lacking. In this work, genomic DNA fragments were obtained from M. oleifera leaves, cloned and completely sequenced, thus revealing new genes encoding Mo-CBP3. Moreover, mass spectrometry analysis showed that the mature protein is a complex mixture of isoforms with a remarkable number of molecular mass variants. Using computational predictions and calculations, most (∼86%) of the experimentally determined masses were assigned to amino acid sequences deduced from DNA fragments. The results suggested that the complex mixture of Mo-CBP3 isoforms originates from proteins encoded by closely related genes, whose products undergo different combinations of distinct post-translational modifications, including cleavage at the N- and C-terminal ends of both subunits, cyclization of N-terminal Gln, as well as Pro hydroxylation, Ser/Thr phosphorylation, and Met oxidation. [Display omitted] •Genomic DNA fragments obtained from leaves and encoding new isoforms of Mo-CBP3 were cloned and sequenced.•Mass spectrometry analysis showed that Mo-CBP3 comprises a remarkable number of molecular mass variants.•Most of the observed molecular masses were satisfactorily assigned to amino acid sequences deduced from DNA clones.•The data suggest that Mo-CBP3 isoforms arise from different combinations of post-translational modifications.
ISSN:0981-9428
1873-2690
DOI:10.1016/j.plaphy.2019.05.003