Journal home
Advance online publication
Current issue
Archive
Press releases
Supplements
Focus
Guide to authors
Online submissionOnline submission
Permissions
For referees
Free online issue
Contact the journal
Subscribe
Advertising
work@npg
naturereprints
About this site
For librarians
 
NPG Resources
Nature
Nature Cell Biology
Nature Reviews Molecular Cell Biology
The EMBO Journal
Nature Reports Stem Cells
Nature Reports Avian Flu
NPG Subject areas
Biotechnology
Cancer
Chemistry
Clinical Medicine
Dentistry
Development
Drug Discovery
Earth Sciences
Evolution & Ecology
Genetics
Immunology
Materials Science
Medical Research
Microbiology
Molecular Cell Biology
Neuroscience
Pharmacology
Physics
Browse all publications
Article
Nature Structural Biology  10, 738 - 743 (2003)
Published online: 17 August 2003; | doi:10.1038/nsb965

The mechanical stability of ubiquitin is linkage dependent

Mariano Carrion-Vazquez1, 5, Hongbin Li1, 5, Hui Lu2, Piotr E Marszalek3, Andres F Oberhauser4 & Julio M Fernandez1

1  Department of Biological Sciences, Columbia University, New York, New York 10027, USA.

2  Department of Bioengineering, University of Illinois at Chicago, Chicago, Illinois 60612, USA.

3  Department of Mechanical Engineering and Material Sciences, Duke University, Durham, North Carolina 27708, USA.

4  Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77555, USA.

5  These authors contributed equally to this work.

Correspondence should be addressed to Julio M Fernandez jfernandez@columbia.edu
Ubiquitin chains are formed through the action of a set of enzymes that covalently link ubiquitin either through peptide bonds or through isopeptide bonds between their C terminus and any of four lysine residues. These naturally occurring polyproteins allow one to study the mechanical stability of a protein, when force is applied through different linkages. Here we used single-molecule force spectroscopy techniques to examine the mechanical stability of N-C−linked and Lys48-C−linked ubiquitin chains. We combined these experiments with steered molecular dynamics (SMD) simulations and found that the mechanical stability and unfolding pathway of ubiquitin strongly depend on the linkage through which the mechanical force is applied to the protein. Hence, a protein that is otherwise very stable may be easily unfolded by a relatively weak mechanical force applied through the right linkage. This may be a widespread mechanism in biological systems.

MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated

REVIEWS
Opinion: When ubiquitin meets ubiquitin receptors: a signalling connection
Nature Reviews Molecular Cell Biology Perspective (01 Jun 2003)
 See all 7 matches for Reviews

NEWS AND VIEWS
Finding a protein's Achilles heel
Nature Structural Biology News and Views (01 Sep 2003)

RESEARCH
Mechanical unfolding intermediates in titin modules
Nature Letters to Editor (04 Nov 1999)
Reverse engineering of the giant muscle protein titin
Nature Letters to Editor (29 Aug 2002)
The molecular elasticity of the extracellular matrix protein tenascin
Nature Letters to Editor (14 May 1998)
 See all 22 matches for Research

 Top
Abstract
Previous | Next
Table of contents
Full textFull text
Download PDFDownload PDF
Send to a friendSend to a friend

Open Innovation Challenges

naturejobs

Figures & Tables
See also: News and Views by Matouschek & Bustamante
See also: Article by Brockwell et al.
Export citation
natureproducts

Search buyers guide:

 
ADVERTISEMENT
 
Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
Journal home | Advance online publication | Current issue | Archive | Press releases | Supplements | For authors | Online submission | Permissions | For referees | Free online issue | About the journal | Contact the journal | Subscribe | Advertising | work@npg | naturereprints | About this site | For librarians
Nature Publishing Group, publisher of Nature, and other science journals and reference works©2003 Nature Publishing Group | Privacy policy