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Journal of Bacteriology, August 2008, p. 5517-5521, Vol. 190, No. 15
0021-9193/08/$08.00+0     doi:10.1128/JB.00407-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Clusters of Charged Residues at the C Terminus of MotA and N Terminus of MotB Are Important for Function of the Escherichia coli Flagellar Motor {triangledown}

Edan R. Hosking{dagger} and Michael D. Manson*

Department of Biology, Texas A&M University, College Station, Texas 77843-3258

Received 22 March 2008/ Accepted 28 April 2008

MotA contains a conserved C-terminal cluster of negatively charged residues, and MotB contains a conserved N-terminal cluster of positively charged residues. Charge-altering mutations affecting these residues impair motility but do not diminish Mot protein levels. The motility defects are reversed by second-site mutations targeting the same or partner protein.


* Corresponding author. Mailing address: Department of Biology, Texas A&M University, College Station, TX 77843-3258. Phone: (979) 845-5158. Fax: (979) 845-2891. E-mail: mike{at}mail.bio.tamu.edu

{triangledown} Published ahead of print on 9 May 2008.

{dagger} Present address: Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109.


Journal of Bacteriology, August 2008, p. 5517-5521, Vol. 190, No. 15
0021-9193/08/$08.00+0     doi:10.1128/JB.00407-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




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