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The N-end rule at atomic resolution

Varshavsky, Alexander (2008) The N-end rule at atomic resolution. Nature Structural & Molecular Biology, 15 (12). pp. 1238-1240. ISSN 1545-9985. https://resolver.caltech.edu/CaltechAUTHORS:VARnsmb08

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Abstract

The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. The N-end rule pathway, ubiquitin-dependent in eukaryotes, is also present in prokaryotes, which lack the ubiquitin system. An illuminating new study presents the crystal structure of a bacterial N-end rule recognition component in complex with a peptide containing a cognate degradation signal.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1038/nsmb1208-1238DOIArticle
http://rdcu.be/yymyPublisherFree ReadCube access
ORCID:
AuthorORCID
Varshavsky, Alexander0000-0002-4011-258X
Additional Information:© 2008 Nature Publishing Group. I thank C. Brower, R. Deshaies, D. Finley, M. Hochstrasser, A. Shemorry and W. Tansey for comments. Studies in my laboratory are supported by grants from the US National Institutes of Health, the Ellison Medical Foundation and the Sandler Program for Asthma Research.
Funders:
Funding AgencyGrant Number
NIHUNSPECIFIED
Ellison Medical FoundationUNSPECIFIED
Sandler Program for Asthma ResearchUNSPECIFIED
Subject Keywords:protein; pathway; CLPS; degradation; proteasome; adapter; proteolysis; bacteria; complex; domain
Issue or Number:12
Record Number:CaltechAUTHORS:VARnsmb08
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:VARnsmb08
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:13359
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:23 Apr 2009 20:27
Last Modified:27 Apr 2020 23:05

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