Haemolysin secretion from E coli.

I B Holland; B Kenny; M Blight

doi:10.1016/0300-9084(90)90138-7

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Haemolysin secretion from E coli.

I B Holland·B Kenny·M Blight

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Abstract

Haemolysin (HlyA) secretion from E coli is directed by a specific C-terminal targeting signal, located within the last 27-50 amino acids, with quite novel characteristics. The HlyA molecule is secreted directly to the medium without a periplasmic intermediate or detectable proteolytic processing. The C-terminal domain of HlyA can also be used to promote the secretion of several other E coli and mammalian proteins. HlyD and HlyB are essential for translocation of HlyA to the medium and we propose that these proteins form a transenvelope complex which initially binds the HlyA signal followed by transport of HlyA to the medium. HlyB is a member of a family of membrane proteins engaged in ATP dependent secretion mechanisms conserved in many organisms including man (P-glycoprotein and the CF protein). In this review we discuss the structure, function and regulation of the secretion mechanism.

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Amino Acid Sequence Bacterial Outer Membrane Proteins Bacterial Proteins Biological Transport Carrier Proteins Escherichia coli Escherichia coli Proteins Gene Expression Regulation, Bacterial Genes, Bacterial Hemolysin Proteins Membrane Proteins Membrane Transport Proteins Molecular Sequence Data Multigene Family Protein Processing, Post-Translational Journal Article Research Support, Non-U.S. Gov't Review

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I B Holland, B Kenny, M Blight. Haemolysin secretion from E coli.. https://doi.org/10.1016/0300-9084(90)90138-7

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