Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M002885200 on May 11, 2000

J. Biol. Chem., Vol. 275, Issue 31, 24191-24198, August 4, 2000
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
275/31/24191    most recent
M002885200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Woodbury, R. L.
Right arrow Articles by Randall, L. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Woodbury, R. L.
Right arrow Articles by Randall, L. L.
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?

Complexes between Protein Export Chaperone SecB and SecA
EVIDENCE FOR SEPARATE SITES ON SecA PROVIDING BINDING ENERGY AND REGULATORY INTERACTIONS*

Ronald L. WoodburyDagger §, Traci B. ToppingDagger , Deborah L. DiamondDagger , Dominic SuciuDagger ||, Carol A. Kumamoto**, Simon J. S. HardyDagger Dagger Dagger , and Linda L. RandallDagger §§

From the Dagger  School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660 and the ** Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111

During localization to the periplasmic space or to the outer membrane of Escherichia coli some proteins are dependent on binding to the cytosolic chaperone SecB, which in turn is targeted to the membrane by specific interaction with SecA, a peripheral component of the translocase. Five variant forms of SecB, previously demonstrated to be defective in mediating export in vivo (Gannon, P. M., and Kumamoto, C. A. (1993) J. Biol. Chem. 268, 1590-1595; Kimsey, H. K., Dagarag, M. D., and Kumamoto, C. A. (1995) J. Biol. Chem. 270, 22831-22835) were investigated with respect to their ability to bind SecA both in solution and at the membrane translocase. We present evidence that at least two regions of SecA are involved in the formation of active complexes with SecB. The variant forms of SecB were all capable of interacting with SecA in solution to form complexes with stability similar to that of complexes between SecA and wild-type SecB. However, the variant forms were defective in interaction with a separate region of SecA, which was shown to trigger a change that was correlated to activation of the complex. The region of SecA involved in activation of the complexes was defined as the extreme carboxyl-terminal 21 aminoacyl residues.

* This work was supported in part by Grants GM29798 (to L. L. R.) and GM36415 (to C. A. K.) from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported in part by Biotechnology Training Grant T32-GM08336 from the National Institute of General Medical Sciences.

Current address: Ciphergen Biosystems, Inc., 490 San Antonio Rd., Palo Alto, CA 94306.

|| Current address: Combimatrix Corporation, 34935 Southeast Douglas Ave., Suite #110, Snoqualmie, WA 98065.

Dagger Dagger Current address: Dept. of Biology, University of York, Y01 5DD United Kingdom.

§§ To whom correspondence should be addressed: School of Molecular Biosciences, Washington State University, P. O. Box 644660, Pullman, WA 99164-4660. Tel.: 509-335-6398; Fax: 509-335-9688; E-mail: topping@wsu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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
C. Mao, S. J. S. Hardy, and L. L. Randall
Maximal Efficiency of Coupling between ATP Hydrolysis and Translocation of Polypeptides Mediated by SecB Requires Two Protomers of SecA
J. Bacteriol., February 1, 2009; 191(3): 978 - 984.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Chen, X. Pan, Y. Tang, S. Quan, P. C. Tai, and S.-F. Sui
Full-length Escherichia coli SecA Dimerizes in a Closed Conformation in Solution as Determined by Cryo-electron Microscopy
J. Biol. Chem., October 24, 2008; 283(43): 28783 - 28787.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. E. J. Spelbrink, A. Kolkman, M. Slijper, J. A. Killian, and B. de Kruijff
Detection and Identification of Stable Oligomeric Protein Complexes in Escherichi coli Inner Membranes: A PROTEOMICS APPROACH
J. Biol. Chem., August 5, 2005; 280(31): 28742 - 28748.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
R. S. Ullers, J. Luirink, N. Harms, F. Schwager, C. Georgopoulos, and P. Genevaux
SecB is a bona fide generalized chaperone in Escherichia coli
PNAS, May 18, 2004; 101(20): 7583 - 7588.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
V. Sharma, A. Arockiasamy, D. R. Ronning, C. G. Savva, A. Holzenburg, M. Braunstein, W. R. Jacobs Jr., and J. C. Sacchettini
Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase
PNAS, March 4, 2003; 100(5): 2243 - 2248.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
G. Sapriel, C. Wandersman, and P. Delepelaire
The SecB Chaperone Is Bifunctional in Serratia marcescens: SecB Is Involved in the Sec Pathway and Required for HasA Secretion by the ABC Transporter
J. Bacteriol., January 1, 2003; 185(1): 80 - 88.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y.-T. Chou, J. F. Swain, and L. M. Gierasch
Functionally Significant Mobile Regions of Escherichia coli SecA ATPase Identified by NMR
J. Biol. Chem., December 20, 2002; 277(52): 50985 - 50990.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement