Genetic analyses of processing involving C-terminal cleavage in penicillin-binding protein 3 of Escherichia coli.

@article{Hara1989GeneticAO,
  title={Genetic analyses of processing involving C-terminal cleavage in penicillin-binding protein 3 of Escherichia coli.},
  author={Hiroshi Hara and Yosuke Nishimura and Jiro Kato and Hideyuki Suzuki and Hiromichi Nagasawa and Akinori Suzuki and Yukinori Hirota},
  journal={Journal of bacteriology},
  year={1989},
  volume={171 11},
  pages={5882-9}
}
The processing of Escherichia coli penicillin-binding protein 3 (PBP 3) was investigated by gene manipulation for producing hybrid and truncated PBP 3 molecules. The hybrid PBP 3 was processed when the N-terminal 40 residues of PBP 3 were replaced by the murein lipoprotein signal peptide which lacked the cysteine residue for processing and followed by seven extra linker residues. In contrast, the PBP 3 molecules truncated at Thr-560 (28-residue deletion) or at Thr-497 (91-residue deletion) were… CONTINUE READING
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