In this study the differentially expressed protein population of Penicillium verrucosum grown either in the dark or under light with a wavelength of 450nm has been analyzed. Light of short wavelength led to oxidative stress in the fungal cell; under this condition the mycotoxin biosynthesis revealed a mutual shift from ochratoxin A to citrinin. Using a proteomic approach combining an optimized protein extraction method with 2-dimensional SDS-PAGE followed by HPLC-ESI-TOF-MS/MS mass spectrometric analysis, initially 56 significantly differential proteins (light vs. dark) were detected comprising proteins of a broad range of isoelectric points and molecular masses. In total, 46 proteins could be identified further by database query, most of these proteins are assumed to be involved in response to stress (e.g. antioxidative proteins, heat shock proteins) and general metabolic processes (e.g. glycolysis, ATP supply). Proteome analyses are necessary to unravel the regulation of secondary metabolite biosynthesis at a translational level. This may enable identification of proteins which are involved in mycotoxin biosynthesis, adaption processes or even stress compensation mechanisms. This study depicts the first proteome analysis of P. verrucosum.
Keywords: Citrinin; Light; Ochratoxin; Oxidative stress; Penicillium verrucosum; Proteome analysis.
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