Showing papers by "Chris A. Kaiser published in 1998"
TL;DR: It is concluded that Ero1p functions in a novel mechanism that sustains the ER oxidizing potential, supporting net formation of protein disulfide bonds in a temperature-sensitive ero1-1 mutant.
482 citations
TL;DR: Two crucial aspects of transport vesicles function have recently been reconstituted using purified proteins and chemically defined lipid bilayers, and bilayer fusion based on the pairing of proteins in the vesicle and target membrane set the stage to address major unresolved questions.
47 citations
TL;DR: Data indicate that a failure to spliceSAR1 pre-mRNA is the specific cause of the secretion defects in prp2-13 and rse1-1, and imply that Sar1p is a limiting component of the ER-to-Golgi transport machinery and suggest a way that secretory pathway function might be coordinated with the amount of gene expression in a cell.
Abstract: Secretory proteins in eukaryotic cells are transported to the cell surface via the endoplasmic reticulum (ER) and the Golgi apparatus by membrane-bounded vesicles. We screened a collection of temperature-sensitive mutants of Saccharomyces cerevisiae for defects in ER-to-Golgi transport. Two of the genes identified in this screen were PRP2, which encodes a known pre-mRNA splicing factor, and RSE1, a novel gene that we show to be important for pre-mRNA splicing. Both prp2-13 and rse1-1 mutants accumulate the ER forms of invertase and the vacuolar protease CPY at restrictive temperature. The secretion defect in each mutant can be suppressed by increasing the amount of SAR1, which encodes a small GTPase essential for COPII vesicle formation from the ER, or by deleting the intron from the SAR1 gene. These data indicate that a failure to splice SAR1 pre-mRNA is the specific cause of the secretion defects in prp2-13 and rse1-1. Moreover, these data imply that Sar1p is a limiting component of the ER-to-Golgi transport machinery and suggest a way that secretory pathway function might be coordinated with the amount of gene expression in a cell.
29 citations
Patent•
10 Aug 1998TL;DR: In this article, expression systems that make use of Erol to enhance disulfide bond formation and thereby to increase the yield of properly folded recombinant proteins are described and discussed.
Abstract: Disclosed herein are expression systems that make use of Erol to enhance disulfide bond formation and thereby to increase the yield of properly folded recombinant proteins. Also disclosed herein are recombinant Erol polypeptides, nucleic acids, vectors, and cells for expressing such polypeptides.
10 citations