Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology
Immunochemical and Mutational Analyses of P-type ATPase Spf1p Involved in the Yeast Secretory Pathway
Chise SUZUKI
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JOURNAL FREE ACCESS

2001 Volume 65 Issue 11 Pages 2405-2411

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Abstract

The yeast SPF1 gene encodes a novel P-type ATPase, the substrate of which specificity has not been identified. It is required for sensitivity to SMKT, a killer toxin produced by the halotolerant yeast Pichia farinosa. To investigate the function of Spf1p, Asp487, the putative phosphorylation site of Spf1p, was replaced by Asn. Expression of the altered SPF1, with Asp487 replaced by Asn, did not suppress the SMKT-resistant phenotype of spf1 mutants, suggesting that the catalytic activity of this ATPase is required for acquisition of sensitivity to SMKT. Subcellular fractionation experiments indicated that the fractionation pattern of Spf1p was similar to that of an early Golgi protein, Och1p. Cells lacking Spf1p had an abnormal fractionation pattern of Sec12p. The spf1 disruptant also showed increased expression of Kar2p and sensitivity to tunicamycin. The glycosylation-defective phenotype and possible role of Spf1p in the secretory pathway are discussed.

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© 2001 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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