Abstract:
: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 and mutated HlyA molecules were analyzed for the ability to be secreted and to lyse erythrocytes. Hemolytic activity absolutely requires the presence of the repeats. The ability of the mutated HlyA molecules to initiate membrane translocation and be secreted required the presence of the C terminus and, to a degree, the repeated amino acid octets.
journal_name
Proc Natl Acad Sci U S Aauthors
Felmlee T,Welch RAdoi
10.1073/pnas.85.14.5269subject
Has Abstractpub_date
1988-07-01 00:00:00pages
5269-73issue
14eissn
0027-8424issn
1091-6490journal_volume
85pub_type
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