ArticleMolecular and cellular biology1999
The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 155 citations in OpenAlex.
- From Isoprene Units to Polyprenols and Dolichols: 70 Years of Polyisoprenoid Biosynthesis Research.Cell biochemistry and biophysics · 2026Review
- The revised three-step detour pathway in dolichol biosynthesis is evolutionarily conserved in budding yeast.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Evolutionary divergence and functional insights into the heteromeric cis-prenyltransferase of Paramecium tetraurelia.The FEBS journal · 2026Article
- Dhdds T206A and Dhdds K42E knock-in mouse models of retinitis pigmentosa 59 are phenotypically similar.Disease models & mechanisms · 2025Article
- The putative prenyltransferase Nus1 is required for filamentation in the human fungal pathogen Candida albicans.G3 (Bethesda, Md.) · 2024Article
- Expression ofJournal of fungi (Basel, Switzerland) · 2022Article
- Vertebrate Animal Models of RP59: Current Status and Future Prospects.International journal of molecular sciences · 2022Review
- Structure-function studies of ultrahigh molecular weight isoprenes provide key insights into their biosynthesis.Communications biology · 2021Article
- Structural elucidation of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Natural rubber biosynthesis in plants, the rubber transferase complex, and metabolic engineering progress and prospects.Plant biotechnology journal · 2019Review
- Inhibition of Dephosphorylation of Dolichyl Diphosphate Alters the Synthesis of Dolichol and Hinders ProteinInternational journal of molecular sciences · 2019Article
- Long-Chain Polyisoprenoids Are Synthesized by AtCPT1 inMolecules (Basel, Switzerland) · 2019Article
- Characterization of aMolecules (Basel, Switzerland) · 2019Article
- Tunicamycin Sensitivity-Suppression by High Gene Dosage Reveals New Functions of the Yeast Hog1 MAP Kinase.Cells · 2019Article
- Molecular Studies of the Protein Complexes InvolvingFrontiers in plant science · 2019Article
- Long-Chain Polyprenols Promote Spore Wall Formation inGenetics · 2017Article
- A conserved C-terminal RThe Journal of biological chemistry · 2017Article
- Polyprenols Are Synthesized by a PlastidialThe Plant cell · 2017Article
- Article
- Identification of Genes inG3 (Bethesda, Md.) · 2017Article
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6 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
As an approach to understand the molecular mechanisms of endoplasmic reticulum (ER) protein sorting, we have isolated yeast rer mutants that mislocalize a Sec12-Mfalpha1p fusion protein from the ER to later compartments of the secretory pathway (S. Nishikawa and A. Nakano, Proc. Natl. Acad. Sci. USA 90:8179-8183, 1993). The temperature-sensitive rer2 mutant mislocalizes different types of ER membrane proteins, suggesting that RER2 is involved in correct localization of ER proteins in general. The rer2 mutant shows several other characteristic phenotypes: slow growth, defects in N and O glycosylation, sensitivity to hygromycin B, and abnormal accumulation of membranes, including the ER and the Golgi membranes. RER2 and SRT1, a gene whose overexpression suppresses rer2, encode novel proteins similar to each other, and their double disruption is lethal. RER2 homologues are found not only in eukaryotes but also in many prokaryote species and thus constitute a large gene family which has been well conserved during evolution. Taking a hint from the phenotype of newly established mutants of the Rer2p homologue of Escherichia coli, we discovered that the rer2 mutant is deficient in the activity of cis-prenyltransferase, a key enzyme of dolichol synthesis. This and other lines of evidence let us conclude that members of the RER2 family of genes encode cis-prenyltransferase itself. The difference in phenotypes between the rer2 mutant and previously obtained glycosylation mutants suggests a novel, as-yet-unknown role of dolichol.
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