Photocontrol of the polypeptide composition of Euglena - Analysis by two-dimensional gel electrophoresis

Abstract

Two-dimensional gel electrophoresis resolved total cellular protein from Euglena gracilis Klebs var. bacillaris Cori into 650 polypeptides detectable by silver staining. Exposure of dark-grown resting Euglena to light for 72 h increased the relative amounts of 79 polypeptides and decreased the relative amounts of 72 polypeptides. Four polypeptides whose level increased upon light exposure were undetectable in the bleached mutant W3BUL. Since W3BUL has lost most if not all of its chloroplast genome, these polypeptides may be coded by the chloroplast genome. Although the majority of the polypeptides studied appear to be coded by the nuclear or mitochondrial genomes, seven polypeptides which were present in W3BUL were not detectable in another chloroplast-DNA-deficient, bleached mutant, W10BSmL. It appears that a number of nonchloroplast genes are no longer expressed in this mutant. Exposure of dark-grown resting cells of the bleached mutant, W3BUL, to light increased the relative amounts of 12 polypeptides and decreased the relative amounts of 14 polypeptides. Since W3BUL lacks detectable protochlorophyll(ide), the chloroplast photoreceptor, the levels of these polypeptides are regulated by light acting through a nonchloroplast photoreceptor. Exposure of cells to light had no detectable effect on the relative amounts of those polypeptides which were present in W10BSmL, even though W10BSmL has a nonchloroplast photoreceptor. Either Euglena contains multiple nonchloroplast photoreceptors, some of which are absent from W10BSmL, or the nonchloroplast photoreceptor present in W10BSmL is uncoupled from some of the events normally controlled by that photoreceptor. © 1983 Springer-Verlag.

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