Evidence for interactions between MotA and MotB, torque-generating elements of the flagellar motor of Escherichia coli.
Cells that overexpress MotA (encoded on a plasmid derived from pBR322) grow slowly because of proton leakage. We have traced this defect to the coexpression of a fusion protein consisting of 60 amino acids from the N terminus of MotB and 50 amino acids specified by pBR322. Mutations within the N terminus, known to abolish function when present in full-length MotB, reversed the growth defect. Growth also was normal when MotA was coexpressed with wild-type MotB or with a series of MotB N-terminal fragments.
Stolz
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Department of Cellular, Harvard University, Cambridge, Massachusetts 02138.
Berg
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D005407:Flagella / Q000378:metabolism*; D015870:Gene Expression; D005816:Genetic Complementation Test; D008969:Molecular Sequence Data; D010957:Plasmids; D014176:Protein Biosynthesis
D001426:Bacterial Proteins; C063010:MotA protein, Bacteria; C064779:MotB protein, Bacteria