Open AccessPhosphorylation of glucosamine‐6‐phosphate synthase is important but not essential for germination and mycelial growth of Candida albicans
Author(s) -
Gabriel Iwona,
Olchowy Jarosław,
StanisławskaSachadyn Anna,
Mio Toshiyuki,
Kur Józef,
Milewski Sławomir
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2004.tb09569.x
Subject(s) - candida albicans , biochemistry , glucosamine , phosphorylation , atp synthase , biology , enzyme , chitin , yeast , chitin synthase , mycelium , kinase , microbiology and biotechnology , botany , chitosan
A site‐directed mutagenesis of the GFA1 gene encoding Candida albicans glucosamine‐6‐phosphate (GlcN‐6‐P) synthase afforded its GFA1S208A version. A product of the modified gene, lacking the putative phosphorylation site for protein kinase A (PKA), exhibited all the basic properties identical to those of the wild‐type enzyme but was no longer a substrate for PKA. Comparison of the C. albicans Δ gfa1/GFA1 and Δ gfa1/GFA1S208A cells, grown under conditions stimulating yeast‐to‐mycelia transformation, revealed that the latter demonstrated lower GlcN‐6‐P synthase specific activity, decreased chitin content and formed much fewer mycelial forms. All these findings, as well as the observed effects of specific inhibitors of protein kinases, suggest that a loss of the possibility of GlcN‐6‐P synthase phosphorylation by PKA strongly reduces but not completely eliminates the germinative response of C. albicans cells.