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Eukaryotic Cell, October 2009, p. 1475-1485, Vol. 8, No. 10
1535-9778/09/$08.00+0 doi:10.1128/EC.00040-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Department of Plant Biology, University of Georgia, Athens, Georgia 30602
Received 1 February 2009/ Accepted 27 July 2009
Protein O-mannosyltransferases (Pmts) initiate O-mannosyl glycan biosynthesis from Ser and Thr residues of target proteins. Fungal Pmts are divided into three subfamilies, Pmt1, -2, and -4. Aspergillus nidulans possesses a single representative of each Pmt subfamily, pmtA (subfamily 2), pmtB (subfamily 1), and pmtC (subfamily 4). In this work, we show that single
pmt mutants are viable and have unique phenotypes and that the
pmtA
pmtB double mutant is the only viable double mutant. This makes A. nidulans the first fungus in which all members of individual Pmt subfamilies can be deleted without loss of viability. At elevated temperatures, all A. nidulans
pmt mutants show cell wall-associated defects and increased sensitivity to cell wall-perturbing agents. The
pmt mutants also show defects in developmental patterning. Germ tube emergence is early in
pmtA and more frequent in
pmtC mutants than in the wild type. In
pmtB mutants, intrahyphal hyphae develop. All
pmt mutants show distinct conidiophore defects. The
pmtA strain has swollen vesicles and conidiogenous cells, the
pmtB strain has swollen conidiophore stalks, and the
pmtC strain has dramatically elongated conidiophore stalks. We also show that AN5660, an ortholog of Saccharomyces cerevisiae Wsc1p, is modified by PmtA and PmtC. The
pmt phenotypes at elevated temperatures, increased sensitivity to cell wall-perturbing agents and restoration to wild-type growth with osmoticum suggest that A. nidulans Pmts modify proteins in the cell wall integrity pathway. The altered developmental patterns in
pmt mutants suggest that A. nidulans Pmts modify proteins that serve as spatial cues.
Published ahead of print on 7 August 2009.
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