When illuminated by visible light, cell-free extracts from the fungus Trichoderma viride catalysed the phosphorylation of at least two proteins with molecular masses of 18 and I14 kDa which were practically absent when the phosphorylation was performed in the dark. The effect of light could be substituted by 3mM cyclic AMP, not only in the cell-free extract, but also in the separated cytosol. It is concluded that the process of photoinduced conidiation in Trichoderma involves phosphorylation of conidiation-specific proteins by (a) cyclic AMP-dependent protein kinase(s) present in the cytosol.
The effect of light on adenyl cyclase (E.C. 4.6.1.1) and 3′:5′‐cyclic‐AMP‐phosphodiesterase (E.C. 3.1.4.17) activity of Trichoderma viride was investigated. Adenyl cyclase proved to be a membrane‐associated enzyme, requiring Mn2+ and was activated by light. In contrast, 3′:5′‐cyclic‐AMP‐phosphodiesterase showed no light‐stimulated activity. The activity of 3′:5′‐cyclic‐AMP‐phosphodiesterase was present mainly in the cytosol and was stimulated by Mg2+.
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