Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on February 24, 2006
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
281/8/4911    most recent
M505453200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Segatori, L.
Right arrow Articles by Georgiou, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Segatori, L.
Right arrow Articles by Georgiou, G.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print November 9, 2005
J. Biol. Chem, 10.1074/jbc.M505453200
Submitted on May 18, 2005
Revised on October 27, 2005
Accepted on November 9, 2005

Conserved role of the linker alpha -helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB

Laura Segatori, Lori Murphy, Silvia Arredondo, Hiroshi Kadokura, Hiram Gilbert, Jon Beckwith, and George Georgiou

Chemical Engineering, University of Texas at Austin, Austin, TX 78712-1095

Corresponding Author: laurasegatori{at}hotmail.com

In the bacterial periplasm the co-existence of a catalyst of disulfide bond formation (DsbA) that is maintained in an oxidized state and of a reduced enzyme that catalyzes the rearrangement of mispaired cysteine residues (DsbC) is important for the folding of proteins containing multiple disulfide bonds. The kinetic partitioning of the DsbA/DsbB and DsbC/DsbD pathways partly depends on the ability of DsbB to oxidize DsbA at rates >1,000 times greater than DsbC. We show that the resistance of DsbC to oxidation by DsbB is abolished by deletions of one or more amino acids within the -helix that connects the N-terminal dimerization domain with the C-terminal thioredoxin domain. As a result, mutant DsbC carrying -helix deletions could catalyze disulfide bond formation and complemented the phenotypes of dsbA cells. Examination of DsbC homologs from H. influenzae, P. aeruginosa, E. chrysanthemi, Y. pseudotuberculosis, and V. cholera (30-70% sequence identity with the E. coli enzyme) revealed that the mechanism responsible for avoiding oxidation by DsbB is a general property of DsbC family enzymes. In addition we found that deletions in the linker region reduced, but did not abolish, the ability of DsbC to assist the formation of active vtPA and phytase in vivo, in a DsbD-dependent manner, revealing that interactions between DsbD and DsbC are also conserved.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
S. Arredondo, L. Segatori, H. F. Gilbert, and G. Georgiou
De Novo Design and Evolution of Artificial Disulfide Isomerase Enzymes Analogous to the Bacterial DsbC
J. Biol. Chem., November 14, 2008; 283(46): 31469 - 31476.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T.-T. Mac, A. von Hacht, K.-C. Hung, R. J. Dutton, D. Boyd, J. C. A. Bardwell, and T. S. Ulmer
Insight into Disulfide Bond Catalysis in Chlamydia from the Structure and Function of DsbH, a Novel Oxidoreductase
J. Biol. Chem., January 11, 2008; 283(2): 824 - 832.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Hiniker, G. Ren, B. Heras, Y. Zheng, S. Laurinec, R. W. Jobson, J. A. Stuckey, J. L. Martin, and J. C. A. Bardwell
Laboratory evolution of one disulfide isomerase to resemble another
PNAS, July 10, 2007; 104(28): 11670 - 11675.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement