Clusters of Charged Residues at the C-terminus of MotA and N-terminus of MotB Are Important for Function of the E. coli Flagellar Motor

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

^* To whom correspondence should be addressed. Email: mike{at}mail.bio.tamu.edu.

	Abstract

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.