This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Steinke, A.
Right arrow Articles by Ehrmann, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Steinke, A.
Right arrow Articles by Ehrmann, M.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2001, p. 375-381, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.375-381.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of Transmembrane Segments 3, 4, and 5 of MalF by Mutational Analysis

Angelika Steinke,1 Sandra Grau,1,dagger Amy Davidson,2 Eckhard Hofmann,1 and Michael Ehrmann1,*

Fakultät für Biologie,Universität Konstanz,78434 Konstanz, Germany,1 and Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 770302

Received 19 July 2000/Accepted 6 October 2000

MalF and MalG are the cytoplasmic membrane components of the binding protein-dependent ATP binding cassette maltose transporter in Escherichia coli. They are thought to form the transport channel and are thus of critical importance for the mechanism of transport. To study the contributions of individual transmembrane segments of MalF, we isolated 27 point mutations in membrane-spanning segments 3, 4, and 5. These data complement a previous study, which described the mutagenesis of membrane-spanning segments 6, 7, and 8. While most of the isolated mutations appear to cause assembly defects, L323Q in helix 5 could interfere more directly with substrate specificity. The phenotypes and locations of the mutations are consistent with a previously postulated structural model of MalF.

* Corresponding author. Mailing address: School of Biosciences, Cardiff University, Museum Ave., P.O. Box 911, Cardiff CF10 3US, United Kingdom. Phone and fax: 44/29/2087 4648. E-mail: ehrmann{at}cf.ac.uk.

dagger Present address: School of Biosciences, Cardiff University, Cardiff CF10 3US, United Kingdom.

Journal of Bacteriology, January 2001, p. 375-381, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.375-381.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Davidson, A. L., Dassa, E., Orelle, C., Chen, J. (2008). Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems. Microbiol. Mol. Biol. Rev. 72: 317-364 [Abstract] [Full Text]  
  • Daus, M. L., Landmesser, H., Schlosser, A., Muller, P., Herrmann, A., Schneider, E. (2006). ATP Induces Conformational Changes of Periplasmic Loop Regions of the Maltose ATP-binding Cassette Transporter. J. Biol. Chem. 281: 3856-3865 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»