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A phosphorylation code of the Aspergillus nidulans global regulator VelvetA (VeA) determines specific functions
Author(s) -
Rauscher Stefan,
Pacher Sylvia,
Hedtke Maren,
Kniemeyer Olaf,
Fischer Reinhard
Publication year - 2016
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13275
Subject(s) - aspergillus nidulans , biology , regulator , phosphorylation , response regulator , microbiology and biotechnology , biochemistry , bacterial protein , mutant , gene
Summary The velvet protein VeA is a global fungal regulator for morphogenetic pathways as well as for the control of secondary metabolism. It is found exclusively in filamentous fungi, where it fulfills conserved, but also unique functions in different species. The involvement of VeA in various morphogenetic and metabolic pathways is probably due to spatially and timely controlled specific protein–protein interactions with other regulators such as phytochrome ( FphA ) or velvet‐like proteins ( VelB ). Here we present evidence that A spergillus nidulans VeA is a multi‐phosphorylated protein and hypothesize that at least four specific amino acids ( T 167, T 170, S 183 and Y 254) undergo reversible phosphorylation to trigger development and sterigmatocystin biosynthesis. Double mutation of T 167 to valine and T 170 to glutamic acid exerted the largest effects with regards to sexual development and veA gene expression. In comparison with wild‐type VeA , which shuttles out of the nuclei after illumination this VeA variant showed stronger nuclear accumulation than the wild type, independent of the light conditions. The interaction between VeA and VelB or FphA , respectively, was affected in the T167V‐T170E mutant. Our results suggest complex regulation of the phosphorylation status of the VeA protein.