Open AccessCloning and characterization of a Neurospora crassa gene required for (1,3) beta-glucan synthase activity and cell wall formation.
Author(s) -
Carol S. Enderlin,
Claude P. Selitrennikoff
Publication year - 1994
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.91.20.9500
Subject(s) - neurospora crassa , complementation , biology , biochemistry , microbiology and biotechnology , mutant , peptide sequence , atp synthase , open reading frame , gene , complementary dna
The glucan synthase 1 gene (gs-1) is required for (1,3) beta-glucan synthase activity [E.C. 2.4.1.34; UDP glucose:1,3-beta-D-glucan 3-beta-D-glucosyltransferase] and for cell wall formation. The gs-1 gene was cloned by functional complementation of the cell-wall-less defect of the (1,3) beta-glucan synthase-deficient mutant, TM1, by using a genomic Neurospora crassa cosmid library. A 2568-nucleotide gs-1 cDNA sequence revealed a 532-amino acid open reading frame encoding a polypeptide of 59 kDa. The predicted gs-1 gene product has no obvious signal peptide cleavage sites or transmembrane domains. A gs-1 null mutant is defective for cell wall formation and (1,3) beta-glucan synthase activity. The predicted GS-1 protein is weakly homologous to a putative Saccharomyces cerevisiae transcriptional regulatory protein.