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Protein secretion by heterologous bacterial ABC‐transporters: the C‐terminus secretion signal of the secreted protein confers high recognition specificity
Author(s) -
Duong F.,
Lazdunski A.,
Murgier M.
Publication year - 1996
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1996.tb02555.x
Subject(s) - secretion , biology , complementation , signal peptide , atp binding cassette transporter , heterologous , transporter , secretory protein , biochemistry , extracellular , peptide sequence , gene , phenotype
Summary Pseudomonas aeruginosa releases several extracellular proteins which are secreted via two independent secretion pathways. Alkaline protease (AprA) is released by its own specific secretion machinery which is an ABC‐transporter. Despite sequence similarities between components of ABC‐transporters in different bacteria, each transporter is dedicated to the secretion of a particular protein or a family of closely related proteins. Heterologous complementation between ABC‐transporters for unrelated polypeptides can occur, but only at a very low level. We show that the 50 C‐terminal amino acids of AprA constitute an autonomous secretion signal. By heterologous complementation experiments between the unrelated a‐haemolysin (HlyA) and Apr secretion systems we demonstrated that it is only the recognition of the secretion signal by the trans‐locator which confers specificity to the secretion process. Secretion was size‐dependent. However inclusion of glycine‐rich repeats from HlyA in AprA seems to overcome the size limitation exerted by the Apr secretion apparatus such that the machinery secreted a hybrid protein 20kDa larger than the normal maximal size.