Effective selenium detoxification in the seed proteins of a hyperaccumulator plant: the analysis of selenium-containing proteins of monkeypot nut (Lecythis minor) seeds.

A shotgun proteomic approach was applied to characterize the selenium (Se)-containing proteins of the selenium hyperaccumulator monkeypot nut (Lecythis minor) seeds. The exceptionally high Se content (>4,000 mg kg(-1)) of the sample enabled a straightforward procedure without the need for multiple preconcentration and fractionation steps. The proteins identified were sulfur-rich seed proteins, namely, 11S globulin (Q84ND2), 2S albumin (B6EU54), 2S sulfur-rich seed storage proteins (P04403 and P0C8Y8) and a 11S globulin-like protein (A0EM48). Database directed search for theoretically selenium-containing peptides was assisted by manual spectra evaluation to achieve around 25% coverage on sulfur analogues. Remarkable detoxification mechanisms on the proteome level were revealed in the form of multiple selenomethionine-methionine substitution and the lack of selenocysteine residues. The degree of selenomethionine substitution could be characterized by an exponential function that implies the inhibition of protein elongation by selenomethionine. Our results contribute to the deeper understanding of selenium detoxification procedures in hyperaccumulator plants.