Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli.

@article{Choi1986TrimericSA,
  title={Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli.},
  author={Dong Seog Choi and Hidetoshi Yamada and Takako Mizuno and Shoji Mizushima},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 19},
  pages={
          8953-7
        }
}
A hybrid gene consisting of the ompF promoter, the coding regions for the signal peptide, and the Ala-Glu residue of the OmpF NH2 terminus and the coding region for the major outer membrane lipoprotein devoid of the NH2-terminal cysteine residue was constructed. Escherichia coli carrying the cloned gene produced the predicted hybrid protein that is the same as the major lipoprotein except that the diacyl glycerylcysteine residue at the NH2 terminus is replaced by the Ala-Glu residue. The hybrid… CONTINUE READING
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