JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 Ma, L.-Y.
Right arrow Articles by Rothfield, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ma, L.-Y.
Right arrow Articles by Rothfield, L.
Journal of Bacteriology, August 2003, p. 4948-4955, Vol. 185, No. 16
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.16.4948-4955.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Mapping the MinE Site Involved in Interaction with the MinD Division Site Selection Protein of Escherichia coli

Lu-Yan Ma,1 Glenn King,1,2 and Lawrence Rothfield1*

Departments of Microbiology,1 Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 060322

Received 31 January 2003/ Accepted 2 May 2003

Interactions between the MinD and MinE proteins are required for proper placement of the Escherichia coli division septum. The site within MinE that is required for interaction with MinD was mapped by studying the effects of site-directed minE mutations on MinD-MinE interactions in yeast two-hybrid and three-hybrid experiments. This confirmed that the MinE N-terminal domain is responsible for the interaction of MinE with MinD. Mutations that interfered with the interaction defined an extended surface on one face of the {alpha}-helical region of the MinE N-terminal domain, consistent with the idea that the MinE-MinD interaction involves formation of a coiled-coil structure by interaction with a complementary helical surface within MinD.


* Corresponding author. Mailing address: Department of Microbiology, University of Connecticut Health Center, Farmington, CT 06032. Phone: (860) 679-3581. Fax: (860) 679-1239. E-mail: lroth{at}neuron.uchc.edu.


Journal of Bacteriology, August 2003, p. 4948-4955, Vol. 185, No. 16
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.16.4948-4955.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2003 by the American Society for Microbiology. All rights reserved.