Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion.

@article{Felmlee1988AlterationsOA,
  title={Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion.},
  author={Theron L. Felmlee and R A Welch},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1988},
  volume={85 14},
  pages={
          5269-73
        }
}
The primary structure of the Escherichia coli hemolysin polypeptide (HlyA) is used to predict intramolecular structures involved in the secretion and cytolytic activity of the molecule. The C-terminal region of HlyA contains a repeated, 8-amino acid chain represented by the consensus sequence Leu-Xaa-Gly-Gly-Xaa-Gly-Asn-Asp. Three in vitro derived mutations of hlyA are described that encode molecules missing various portions of the C-terminal region, including the repeat region. The wild-type… CONTINUE READING
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