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

作者：Barbara Stolz, Howard C. Berg · 发表于：Journal of Bacteriology · 年份：1991 · DOI：10.1128/jb.173.21.7033-7037.1991 · 被引用次数：152 · 研究领域：Bacterial Genetics and Biotechnology、Photosynthetic Processes and Mechanisms、Escherichia coli research studies

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.