This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tachibana, C Articles by Stevens, T H Search for Related Content PubMed PubMed Citation Articles by Tachibana, C Articles by Stevens, T H

 Previous Article  |  Next Article 

Mol Cell Biol. 1992 October; 12(10): 4601-4611

The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase.

Institute of Molecular Biology, University of Oregon, Eugene 97403.

ABSTRACT

The product of the EUG1 gene of Saccharomyces cerevisiae is a soluble endoplasmic reticulum protein with homology to both the mammalian protein disulfide isomerase (PDI) and the yeast PDI homolog encoded by the essential PDI1 gene. Deletion or overexpression of EUG1 causes no growth defects under a variety of conditions. EUG1 mRNA and protein levels are dramatically increased in response to the accumulation of native or unglycosylated proteins in the endoplasmic reticulum. Overexpression of the EUG1 gene allows yeast cells to grow in the absence of the PDI1 gene product. Depletion of the PDI1 protein in Saccharomyces cerevisiae causes a soluble vacuolar glycoprotein to accumulate in its endoplasmic reticulum form, and this phenotype is only partially relieved by the overexpression of EUG1. Taken together, our results indicate that PDI1 and EUG1 encode functionally related proteins that are likely to be involved in interacting with nascent polypeptides in the yeast endoplasmic reticulum.

This article has been cited by other articles:

• Tai, S. L., Snoek, I., Luttik, M. A. H., Almering, M. J. H., Walsh, M. C., Pronk, J. T., Daran, J.-M. (2007). Correlation between transcript profiles and fitness of deletion mutants in anaerobic chemostat cultures of Saccharomyces cerevisiae. Microbiology 153: 877-886 [Abstract] [Full Text]  
• Wentz, A. E., Shusta, E. V. (2007). A Novel High-Throughput Screen Reveals Yeast Genes That Increase Secretion of Heterologous Proteins. Appl. Environ. Microbiol. 73: 1189-1198 [Abstract] [Full Text]  
• Kulp, M. S., Frickel, E.-M., Ellgaard, L., Weissman, J. S. (2006). Domain Architecture of Protein-disulfide Isomerase Facilitates Its Dual Role as an Oxidase and an Isomerase in Ero1p-mediated Disulfide Formation. J. Biol. Chem. 281: 876-884 [Abstract] [Full Text]  
• Kimura, T., Hosoda, Y., Sato, Y., Kitamura, Y., Ikeda, T., Horibe, T., Kikuchi, M. (2005). Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J. Biol. Chem. 280: 31438-31441 [Abstract] [Full Text]  
• Xiao, R., Wilkinson, B., Solovyov, A., Winther, J. R., Holmgren, A., Lundstrom-Ljung, J., Gilbert, H. F. (2004). The Contributions of Protein Disulfide Isomerase and Its Homologues to Oxidative Protein Folding in the Yeast Endoplasmic Reticulum. J. Biol. Chem. 279: 49780-49786 [Abstract] [Full Text]  
• Solovyov, A., Xiao, R., Gilbert, H. F. (2004). Sulfhydryl Oxidation, Not Disulfide Isomerization, Is the Principal Function of Protein Disulfide Isomerase in Yeast Saccharomyces cerevisiae. J. Biol. Chem. 279: 34095-34100 [Abstract] [Full Text]  
• Roberts, D. G. W., Lamb, M. R., Dieckmann, C. L. (2001). Characterization of the EYE2 Gene Required for Eyespot Assembly in Chlamydomonas reinhardtii. Genetics 158: 1037-1049 [Abstract] [Full Text]  
• Fetrow, J. S., Siew, N., Di Gennaro, J. A., Martinez-Yamout, M., Dyson, H. J., Skolnick, J. (2001). Genomic-scale comparison of sequence- and structure-based methods of function prediction: Does structure provide additional insight?. Protein Sci. 10: 1005-1014 [Abstract] [Full Text]  
• Norgaard, P., Westphal, V., Tachibana, C., Alsoe, L., Holst, B., Winther, J. R. (2001). Functional Differences in Yeast Protein Disulfide Isomerases. J. Cell Biol. 152: 553-562 [Abstract] [Full Text]  
• Locke, E. G., Bonilla, M., Liang, L., Takita, Y., Cunningham, K. W. (2000). A Homolog of Voltage-Gated Ca2+ Channels Stimulated by Depletion of Secretory Ca2+ in Yeast. Mol. Cell. Biol. 20: 6686-6694 [Abstract] [Full Text]  
• Ng, D. T.W., Spear, E. D., Walter, P. (2000). The Unfolded Protein Response Regulates Multiple Aspects of Secretory and Membrane Protein Biogenesis and Endoplasmic Reticulum Quality Control. J. Cell Biol. 150: 77-88 [Abstract] [Full Text]  
• Gillece, P., Luz, J. M., Lennarz, W. J., de la Cruz, F. J., Romisch, K. (1999). Export of a Cysteine-free Misfolded Secretory Protein from the Endoplasmic Reticulum for Degradation Requires Interaction with Protein Disulfide Isomerase. J. Cell Biol. 147: 1443-1456 [Abstract] [Full Text]  
• Gilstring, C. F., Melin-Larsson, M., Ljungdahl, P. O. (1999). Shr3p Mediates Specific COPII Coatomer-Cargo Interactions Required for the Packaging of Amino Acid Permeases Into ER-derived Transport Vesicles. Mol. Biol. Cell 10: 3549-3565 [Abstract] [Full Text]  
• Kane, P. M., Tarsio, M., Liu, J. (1999). Early Steps in Assembly of the Yeast Vacuolar H+-ATPase. J. Biol. Chem. 274: 17275-17283 [Abstract] [Full Text]  
• Mori, K., Ogawa, N., Kawahara, T., Yanagi, H., Yura, T. (1998). Palindrome with Spacer of One Nucleotide Is Characteristic of the cis-Acting Unfolded Protein Response Element in Saccharomyces cerevisiae. J. Biol. Chem. 273: 9912-9920 [Abstract] [Full Text]  
• Jackson, D. D., Stevens, T. H. (1997). VMA12 Encodes a Yeast Endoplasmic Reticulum Protein Required for Vacuolar H+-ATPase Assembly. J. Biol. Chem. 272: 25928-25934 [Abstract] [Full Text]  
• Kawahara, T., Yanagi, H., Yura, T., Mori, K. (1997). Endoplasmic Reticulum Stress-induced mRNA Splicing Permits Synthesis of Transcription Factor Hac1p/Ern4p That Activates the Unfolded Protein Response. Mol. Biol. Cell 8: 1845-1862 [Abstract] [Full Text]  
• Holst, B., Tachibana, C., Winther, J. R. (1997). Active Site Mutations in Yeast Protein Disulfide Isomerase Cause Dithiothreitol Sensitivity and a Reduced Rate of Protein Folding in the Endoplasmic Reticulum. J. Cell Biol. 138: 1229-1238 [Abstract] [Full Text]  
• Laboissière, M. C. A., Sturley, S. L., Raines, R. T. (1995). The Essential Function of Protein-disulfide Isomerase Is to Unscramble Non-native Disulfide Bonds. J. Biol. Chem. 270: 28006-28009 [Abstract] [Full Text]  
• Roy, S. N., Kudryk, B., Redman, C. M. (1995). Secretion of Biologically Active Recombinant Fibrinogen by Yeast. J. Biol. Chem. 270: 23761-23767 [Abstract] [Full Text]  
• Hill, K. J., Stevens, T. H. (1995). Vma22p Is a Novel Endoplasmic Reticulum-associated Protein Required for Assembly of the Yeast Vacuolar H[IMAGE]-ATPase Complex. J. Biol. Chem. 270: 22329-22336 [Abstract] [Full Text]  
• Lundström-Ljung, J., Holmgren, A. (1995). Glutaredoxin Accelerates Glutathione-dependent Folding of Reduced Ribonuclease A Together with Protein Disulfide-isomerase. J. Biol. Chem. 270: 7822-7828 [Abstract] [Full Text]  
• Jannatipour, M., Rokeach, L. A. (1995). The Schizosaccharomyces pombe Homologue of the Chaperone Calnexin Is Essential for Viability. J. Biol. Chem. 270: 4845-4853 [Abstract] [Full Text]  
• Caldwell, S. R., Hill, K. J., Cooper, A. A. (2001). Degradation of Endoplasmic Reticulum (ER) Quality Control Substrates Requires Transport between the ER and Golgi. J. Biol. Chem. 276: 23296-23303 [Abstract] [Full Text]