JBC

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


     

A more recent version of this article appeared on November 21, 2001
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
276/48/44751    most recent
M108729200v1
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chen, Q.
Right arrow Articles by Amster-Choder, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chen, Q.
Right arrow Articles by Amster-Choder, O.
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 September 28, 2001
J. Biol. Chem, 10.1074/jbc.M108729200
Submitted on September 11, 2001
Revised on September 25, 2001
Accepted on September 27, 2001

A Novel Sugar - Stimulated Covalent Switch in a Sugar sensor

Qing Chen, Anat Nussbaum-Shochat, and Orna Amster-Choder

Molecular Biology, Hebrew University, Hadassah Medical School, Jerusalem 91120

Corresponding Author: amster{at}cc.huji.ac.il

The bgl sensory system is composed of a membrane-bound sugar-sensor, BglF, and a transcriptional regulator, BglG. The sensor BglF has several enzymatic activities: in its non-stimulated state, it acts as BglG phosphorylase; in the presence of beta -glucoside in the growth medium, it acts as BglG dephosphorylase and as the beta -glucoside phosphotransferase. The same active site on BglF, Cys-24, is responsible for the phosphorylation of both the stimulating sugar and the BglG protein. BglF, is composed of three domains, two hydrophilic and one hydrophobic. Our previous results suggested that catalysis of the sugar-stimulated functions depends on specific interactions between the B domain, which contains the active site cysteine, and the integral membrane C domain. We report here that the stimulating sugar triggers the formation of a disulfide bond between the active site cysteine and another cysteine in the membrane-embedded domain of BglF. Inability of a mutant BglF protein to form the disulfide bridge between the B and C domains correlates with its inability to catalyze the sugar-stimulated functions. The ability of the cysteine residue in BglF to bind covalently either to a phosphoryl group or to another cysteine residue, depending on the protein stimulation state, suggests a novel way to control signaling by alternative bond formation.


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. Bacteriol.Home page
G. Monderer-Rothkoff and O. Amster-Choder
Genetic Dissection of the Divergent Activities of the Multifunctional Membrane Sensor BglF
J. Bacteriol., December 1, 2007; 189(23): 8601 - 8615.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Yagur-Kroll and O. Amster-Choder
Dynamic Membrane Topology of the Escherichia coli {beta}-Glucoside Transporter BglF
J. Biol. Chem., May 13, 2005; 280(19): 19306 - 19318.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
L. Lopian, A. Nussbaum-Shochat, K. O'Day-Kerstein, A. Wright, and O. Amster-Choder
The BglF sensor recruits the BglG transcription regulator to the membrane and releases it on stimulation
PNAS, June 10, 2003; 100(12): 7099 - 7104.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.