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. 1991 Nov;173(21):7033–7037. doi: 10.1128/jb.173.21.7033-7037.1991

Evidence for interactions between MotA and MotB, torque-generating elements of the flagellar motor of Escherichia coli.

B Stolz 1, H C Berg 1
PMCID: PMC209062  PMID: 1938906

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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