The pH-induced glycosylation of secreted phosphatases is mediated in Aspergillus nidulans by the regulatory gene pacC-dependent pathway

In this communication, we show that the pacC(c)14 mutation drastically reduced the mannose, and N-acetylglycosamine content of the pacA-encoded acid phosphatase secreted by the. fungus Aspergillus, nidulans, when grown at 22degreesC, pH 5.0, compared to a control strain, The staining., after PAGE was not. observed for the pacA-encoded acid phosphatase, while the palD-encoded Pi-repressible alkaline phosphatase had an, altered electrophoretic mobility., In addition, the secreted acid phosphatase also had a reduced number of isoforms visualized by staining after IEF and, grycosylation had a protective effect, against its heat inactivation. We also show that at, full-length version of gene pacC-1, cloned from. Neurospora crassa, complemented the pacC(c) 14 mutation of A. nidulans, including the. remediation of, both the; acid. and alkaline. Pi-repressible. phosphatases secreted at pH 5,0, which indicates that glycosylation, of secreted phosphatases, is mediated in. A.. nidulans by the. conserved PacC pathway that governs. pH-responsive gene expression. (C) 2003 Elsevier Science (USA),. All, rights: reserved.