PMID:2116181
| Citation |
Holland, IB, Kenny, B and Blight, M Haemolysin secretion from E coli. Biochimie 72:131-41 |
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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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| Keywords |
Amino Acid Sequence; Bacterial Outer Membrane Proteins/genetics; Bacterial Proteins/genetics; Bacterial Proteins/secretion; Biological Transport; Carrier Proteins/genetics; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Genes, Bacterial; Hemolysin Proteins/genetics; Hemolysin Proteins/secretion; Membrane Proteins/metabolism; Membrane Transport Proteins; Molecular Sequence Data; Multigene Family; Protein Processing, Post-Translational |
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