HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 49, 48965-48972, December 5, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/49/48965    most recent M307362200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Jiang, F. Articles by Dalbey, R. E. Search for Related Content PubMed PubMed Citation Articles by Jiang, F. Articles by Dalbey, R. E. Social Bookmarking                      What's this?

Defining the Regions of Escherichia coli YidC That Contribute to Activity^*

Fenglei Jiang, Minyong Chen, Liang Yi, Jan-Willem de Gier, Andreas Kuhn¶, and Ross E. Dalbey||

From the Department of Chemistry, Ohio State University, Columbus, Ohio 43210, the Department of Biochemistry and Biophysics, Arrhenius Laboratory, Stockholm University, S-106 91 Stockholm, Sweden, and the ^¶Institute for Microbiology and Molecular Biology, University of Hohenheim, Garbenstrasse 30, D-70599 Stuttgart, Germany

The YidC/Oxa1/Alb3 family of proteins catalyzes membrane protein insertion in bacteria, mitochondria, and chloroplasts. In this study, we investigated which regions of the bacterial YidC protein are important for its function in membrane protein biogenesis. In Escherichia coli, YidC spans the membrane six times, with a large 319-residue periplasmic domain following the first transmembrane domain. We found that this large periplasmic domain is not required for YidC function and that the residues in the exposed hydrophilic loops or C-terminal tail are not critical for YidC activity. Rather, the five C-terminal transmembrane segments that contain the three consensus sequences in the YidC/Oxa1/Alb3 family are important for its function. However, by systematically replacing all the residues in transmembrane segment (TM) 2, TM3, and TM6 with serine and by swapping TM4 and TM5 with unrelated transmembrane segments, we show that the precise sequence of these transmembrane regions is not essential for in vivo YidC activity. Single serine mutations in TM2, TM3, and TM6 impaired the membrane insertion of the Sec-independent procoat-leader peptidase protein. We propose that the five C-terminal transmembrane segments of YidC function as a platform for the translocating substrate protein to support its insertion into the membrane.

Received for publication, July 9, 2003 , and in revised form, September 22, 2003.

^* This work was supported by National Institutes of Health Grant GM63862 (to R. E. D.), by Deutsche Forschungsgemeinschaft Grant Ku 749/3-1 (to A. K.), and by a Swedish Research Council grant (to J.-W. d. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed: Dept. of Chemistry, Ohio State University, 100 W. 18th Ave., Columbus, OH 43210. Tel.: 614-292-2384; Fax: 614-292-1532; E-mail: dalbey{at}chemistry.ohio-state.edu.

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

This article has been cited by other articles:

				S. Kol, N. Nouwen, and A. J. M. Driessen The Charge Distribution in the Cytoplasmic Loop of Subunit C of the F1F0 ATPase Is a Determinant for YidC Targeting J. Biol. Chem., April 11, 2008; 283(15): 9871 - 9877. [Abstract] [Full Text] [PDF]

				S. Ravaud, G. Stjepanovic, K. Wild, and I. Sinning The Crystal Structure of the Periplasmic Domain of the Escherichia coli Membrane Protein Insertase YidC Contains a Substrate Binding Cleft J. Biol. Chem., April 4, 2008; 283(14): 9350 - 9358. [Abstract] [Full Text] [PDF]

				D. C. Oliver and M. Paetzel Crystal Structure of the Major Periplasmic Domain of the Bacterial Membrane Protein Assembly Facilitator YidC J. Biol. Chem., February 22, 2008; 283(8): 5208 - 5216. [Abstract] [Full Text] [PDF]

				J. Yuan, G. J. Phillips, and R. E. Dalbey Isolation of Cold-Sensitive yidC Mutants Provides Insights into the Substrate Profile of the YidC Insertase and the Importance of Transmembrane 3 in YidC Function J. Bacteriol., December 15, 2007; 189(24): 8961 - 8972. [Abstract] [Full Text] [PDF]

				S. Wagner, L. Baars, A. J. Ytterberg, A. Klussmeier, C. S. Wagner, O. Nord, P.-A. Nygren, K. J. van Wijk, and J.-W. de Gier Consequences of Membrane Protein Overexpression in Escherichia coli Mol. Cell. Proteomics, September 1, 2007; 6(9): 1527 - 1550. [Abstract] [Full Text] [PDF]

				S. Meier, W. Neupert, and J. M. Herrmann Proline residues of transmembrane domains determine the sorting of inner membrane proteins in mitochondria J. Cell Biol., September 12, 2005; 170(6): 881 - 888. [Abstract] [Full Text] [PDF]

				E. van Bloois, S. Nagamori, G. Koningstein, R. S. Ullers, M. Preuss, B. Oudega, N. Harms, H. R. Kaback, J. M. Herrmann, and J. Luirink The Sec-independent Function of Escherichia coli YidC Is Evolutionary-conserved and Essential J. Biol. Chem., April 1, 2005; 280(13): 12996 - 13003. [Abstract] [Full Text] [PDF]

				C. Lemaire, F. Guibet-Grandmougin, D. Angles, G. Dujardin, and N. Bonnefoy A Yeast Mitochondrial Membrane Methyltransferase-like Protein Can Compensate for oxa1 Mutations J. Biol. Chem., November 12, 2004; 279(46): 47464 - 47472. [Abstract] [Full Text] [PDF]

				R. E. Dalbey and A. Kuhn YidC family members are involved in the membrane insertion, lateral integration, folding, and assembly of membrane proteins J. Cell Biol., September 13, 2004; 166(6): 769 - 774. [Abstract] [Full Text] [PDF]