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  The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family

Rudolph, H. K., Antebi, A., Fink, G. R., Buckley, C. M., Dorman, T. E., LeVitre, J., et al. (1989). The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family. Cell, 58(1), 133-45.

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Rudolph, H. K., Author
Antebi, A.1, Author           
Fink, G. R., Author
Buckley, C. M., Author
Dorman, T. E., Author
LeVitre, J., Author
Davidow, L. S., Author
Mao, J. I., Author
Moir, D. T., Author
Affiliations:
1Department Antebi - Molecular Genetics of Ageing, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_1942285              

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Free keywords: Amino Acid Sequence Base Sequence Biological Transport, Active Calcium/*physiology Calcium-Transporting ATPases/*genetics Cloning, Molecular Fungal Proteins/*secretion *Genes, Fungal Glycosylation Membrane Proteins/*genetics/ultrastructure Molecular Sequence Data Mutation Protein Conformation Saccharomyces cerevisiae/*metabolism
 Abstract: The genes for two new P-type ATPases, PMR1 and PMR2, have been identified in yeast. A comparison of the deduced sequences of the PMR proteins with other known ion pumps showed that both proteins are very similar to Ca2+ ATPases. PMR1 is identical to SSC1, a gene previously identified by its effect on secretion of some foreign proteins from yeast. Proteins secreted from pmr1 mutants lack the outer chain glycosylation that normally results from passage through the Golgi. Loss of PMR1 function suppresses the lethality of ypt1-1, a mutation that blocks the secretion pathway. These data suggest that PMR1 functions as a Ca2+ pump affecting transit through the secretory pathway.

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 Dates: 1989-06-141989-07-14
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: Other: 2526682
ISSN: 0092-8674 (Print)0092-8674
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Title: Cell
  Alternative Title : Cell
Source Genre: Journal
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Pages: - Volume / Issue: 58 (1) Sequence Number: - Start / End Page: 133 - 45 Identifier: -