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Molecular and Cellular Biology, January 1999, p. 471-483, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Yeast RER2 Gene, Identified by Endoplasmic Reticulum Protein Localization Mutations, Encodes cis-Prenyltransferase, a Key Enzyme in Dolichol Synthesis

Miyuki Sato,1 Ken Sato,1 Shuh-ichi Nishikawa,2 Aiko Hirata,3 Jun-ichi Kato,4 and Akihiko Nakano1,*

Molecular Membrane Biology Laboratory, RIKEN, Wako, Saitama 351-0198,1 Department of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602,2 Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113-0032,3 and Department of Molecular Biology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639,4 Japan

Received 27 July 1998/Returned for modification 11 September 1998/Accepted 16 September 1998

As an approach to understand the molecular mechanisms of endoplasmic reticulum (ER) protein sorting, we have isolated yeast rer mutants that mislocalize a Sec12-Mfalpha 1p 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.

* Corresponding author. Mailing address: Molecular Membrane Biology Lab., RIKEN, Wako, Saitama 351-0198, Japan. Phone: 81-48-467-9547. Fax: 81-48-462-4679. E-mail: nakano{at}postman.riken.go.jp.

Molecular and Cellular Biology, January 1999, p. 471-483, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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