CaltechAUTHORS
  A Caltech Library Service

Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae

Balzi, Elisabetta and Choder, Mordechai and Chen, Weining and Varshavsky, Alexander and Goffeau, Andre (1990) Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae. Journal of Biological Chemistry, 265 (13). pp. 7464-7471. ISSN 0021-9258. doi:10.1016/s0021-9258(19)39136-7. https://resolver.caltech.edu/CaltechAUTHORS:20210129-142402779

[img] PDF - Published Version
Creative Commons Attribution Non-commercial No Derivatives.

4MB

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20210129-142402779

Abstract

Aminoacyl-tRNA-protein transferases (Arg-transferases) catalyze post-translational conjugation of specific amino acids to the amino termini of acceptor proteins. A function of these enzymes in eukaryotes has been shown to involve the conjugation of destabilizing amino acids to the amino termini of short-lived proteins, these reactions being a part of the N-end rule pathway of protein degradation (Gonda, D. K., Bachmair, A., Wünning, I., Tobias, J. W., Lane, W. S., and Varshavsky, A. (1989) J. Biol. Chem. 264, 16700-16712). We have cloned the ATE1 gene of the yeast Saccharomyces cerevisiae which encodes arginyl-tRNA-protein transferase. ATE1 gives rise to a approximately 1.6-kilobase mRNA and codes for a 503-residue protein. Expression of the yeast ATE1 gene in Escherichia coli, which lacks Arg-transferases, was used to show that the ATE1 protein possesses the Arg-transferase activity. Null ate1 mutants are viable but lack the Arg-transferase activity and are unable to degrade those substrates of the N-end rule pathway that start with residues recognized by the Arg-transferase.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1016/s0021-9258(19)39136-7DOIArticle
ORCID:
AuthorORCID
Varshavsky, Alexander0000-0002-4011-258X
Additional Information:© 1990 ASBMB. Under an Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0). Received for publication, December 18, 1989. This work was supported in part by grants from the Services de la Politique Scientifique: Action Science de la Vie and from the Fonds National pour la Recherche Scientifique, Belgium (to A. G.) and by National Institutes of Health Grants GM31530 and DK39520 (to A. V.). The costs of publication of this were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. The nucleotide sequence(s) reported in this paper has been submitted to the GenBank/EMBL Data Bank with accession number(s) J05404. Supported by a postdoctoral fellowship from the Weizmann Foundation. We thank Myriam De Saedeleer for excellent technical assistance; Michael Leibowitz, Stanislaw Ulaszewski, and Francois Lacroute for the gifts of strains and plasmids; Jean Ganglos for communicating the amino acid sequence of the E. coli Arg-tRNA synthetase before publication; and Amanda Melton for advice and assistance with computer analysis of the ATE1 sequence. We also thank members of the MIT laboratory, especially Rohan Baker, Bonnie Bartel, Mark Hochstrasser, and Irene Ota for their comments on the manuscript and Barbara Doran and Michel de Longree for secretarial assistance.
Funders:
Funding AgencyGrant Number
Services de la Politique Scientifique: Action Science de la VieUNSPECIFIED
Fonds de la Recherche Scientifique (FNRS)UNSPECIFIED
NIHGM31530
NIHDK39520
Weizmann FellowshipUNSPECIFIED
Issue or Number:13
DOI:10.1016/s0021-9258(19)39136-7
Record Number:CaltechAUTHORS:20210129-142402779
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20210129-142402779
Official Citation:E Balzi, M Choder, W N Chen, A Varshavsky, A Goffeau, Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae., Journal of Biological Chemistry, Volume 265, Issue 13, 1990, Pages 7464-7471, ISSN 0021-9258, https://doi.org/10.1016/S0021-9258(19)39136-7. (http://www.sciencedirect.com/science/article/pii/S0021925819391367)
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:107817
Collection:CaltechAUTHORS
Deposited By: George Porter
Deposited On:01 Feb 2021 17:00
Last Modified:16 Nov 2021 19:06

Repository Staff Only: item control page