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The isolation of a dol‐P‐man synthase from Ustilago maydis that functions in Saccharomyces cerevisiae
Author(s) -
Zimmerman Janet W.,
Specht Charles A.,
Cazares Beatriz Xoconostle,
Robbins Phillips W.
Publication year - 1996
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/(sici)1097-0061(19960630)12:8<765::aid-yea974>3.0.co;2-a
Subject(s) - ustilago , biology , neurospora crassa , saccharomyces cerevisiae , aspergillus nidulans , biochemistry , neurospora , gene , mannose , candida albicans , microbiology and biotechnology , peptide sequence , genetics , mutant
Genomic DNAs from several fungi were screened for a homologous sequence to Saccharomyces cerevisiae DPM1 , an essential gene which encodes dolichyl phosphoryl mannose synthase. The fungi examined included Aspergillus nidulans, Neurospora crassa, Schizophyllum commune and Ustilago maydis . Only U. maydis gave a significant signal after Southern hybridization using DPM1 as a probe. The Ustilago homolog was subsequently cloned and sequenced. The predicted protein of 294 amino acids has 60% identity to the S. cerevisiae protein, but lacks the putative ‘dolichol recognition sequence’. RNA of ca. 900 bp is transcribed in both yeast and filamentous cells of Ustilago . In Escherichia coli , the U. maydis sequence expressed a 35 kDa protein exhibiting dolichyl phosphoryl mannose synthase activity. The sequence was also shown to complement a haploid strain of S. cerevisiae containing a deletion of the DPM1 gene. The U. maydis sequence therefore, encodes a dolichyl phosphoryl mannose synthase that can support normal vegetative growth in S. cerevisiae . The GenBank accession number is U54797.