HEMOLYSIN SECRETION FROM ESCHERICHIA-COLI

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. © 1990.