A Caltech Library Service

Yeast N-terminal Amidase: a new enzyme and component of the N-end rule pathway

Baker, Rohan T. and Varshavsky, Alexander (1995) Yeast N-terminal Amidase: a new enzyme and component of the N-end rule pathway. Journal of Biological Chemistry, 270 (20). pp. 12065-12074. ISSN 0021-9258. doi:10.1074/jbc.270.20.12065.

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


Use this Persistent URL to link to this item:


The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. Tertiary destabilizing N-terminal residues asparagine and glutamine function through their conversion, by enzymatic deamidation, into the secondary destabilizing residues aspartate and glutamate, whose activity requires their enzymatic conjugation to arginine, one of the primary destabilizing residues. We isolated a Saccharomyces cerevisiae gene, termed NTA1, that encodes an amidase (Nt-amidase) specific for N-terminal asparagine and glutamine. Alterations at the putative active-site cysteine of the 52-kDa Nt-amidase inactivate the enzyme. Null nta1 mutants are viable but unable to degrade N-end rule substrates that bear N-terminal asparagine or glutamine. The effects of overexpressing Nt-amidase and other components of the N-end rule pathway suggest interactions between these components and the existence of a multienzyme targeting complex.

Item Type:Article
Related URLs:
URLURL TypeDescription
Varshavsky, Alexander0000-0002-4011-258X
Additional Information:© 1995 American Society for Biochemistry and Molecular Biology. Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0). Received for publication, January 10, 1995, and in revised form, March 9, 1995. This work was supported by Grants DK39520 and GM31530 from the National Institutes of Health (to A. V.). The costs of publication of this article 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™/EMEL Data Bank with accession number(s) L35564. Supported by fellowships from the Fulbright Foundation and the Life Sciences Research Foundation. We thank S. Grigoryev for his advice about the in vitro deamidation assay and B. Bartel, M. Hochstrasser, and K. Madura for helpful discussions.
Funding AgencyGrant Number
Fulbright FoundationUNSPECIFIED
Life Sciences Research FoundationUNSPECIFIED
Issue or Number:20
Record Number:CaltechAUTHORS:20210211-152331656
Persistent URL:
Official Citation:Rohan T. Baker, Alexander Varshavsky, Yeast N-terminal Amidase: A NEW ENZYME AND COMPONENT OF THE N-END RULE PATHWAY, Journal of Biological Chemistry, Volume 270, Issue 20, 1995, Pages 12065-12074, ISSN 0021-9258,
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:108017
Deposited By: George Porter
Deposited On:12 Feb 2021 15:26
Last Modified:16 Nov 2021 19:08

Repository Staff Only: item control page