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Volume 270, Number 6, Issue of February 10, 1995 pp. 2770-2775
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Protein O-Glycosylation in Yeast
THE PMT2 GENE SPECIFIES A SECOND PROTEIN O-MANNOSYLTRANSFERASE THAT FUNCTIONS IN ADDITION TO THE PMT1-ENCODED ACTIVITY

(Received for publication, October 20, 1994; and in revised form, November 30, 1994)

Marc Lussier Martina Gentzsch Anne-Marie Sdicu Howard Bussey Widmar Tanner

The PMT2 gene from Saccharomyces cerevisiae was identified as FUN25, a transcribed open reading frame on the left arm of chromosome I (Ouellette, B. F. F., Clark, M. W. C., Keng, T., Storms, R. G., Zhong, W., Zeng, B., Fortin, N., Delaney, S., Barton, A., Kaback, D. B., and Bussey, H.(1993) Genome 36, 32-42). The product encoded by the PMT2 gene shows significant similarity with the dolichyl phosphate-D-mannose:protein O-D-mannosyltransferase, Pmt1p (EC 2.4.1.109), which is required for initiating the assembly of O-linked oligosaccharides in S. cerevisiae (Strahl-Bolsinger, S., Immervoll, T., Deutzmann, R., and Tanner, W.(1993) Proc. Natl. Acad. Sci. U. S. A. 90, 8164-8168). The PMT2 gene encodes a new protein O-D-mannosyltransferase. Yeast cells carrying a PMT2 disruption show a diminished in vitro and in vivo O-mannosylation activity and resemble mutants with a nonfunctional PMT1 gene. Strains bearing a pmt1 pmt2 double disruption show a severe growth defect but retain residual O-mannosylation activity indicating the presence of at least one more protein-O-mannosyltransferase.




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