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PMID: 2839840 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 85 ·No. 14 ·1988-07-00 ·Pages 5269-73

Felmlee T, Welch RA

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.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/genetics,metabolism Base Sequence DNA Restriction Enzymes DNA, Bacterial/genetics DNA, Recombinant Endopeptidase K Escherichia coli/analysis,genetics Escherichia coli Proteins Hemolysin Proteins Hemolysis Molecular Sequence Data Mutation Plasmids Repetitive Sequences, Nucleic Acid Serine Endopeptidases/metabolism Structure-Activity Relationship
Chemicals
Bacterial Proteins DNA, Bacterial DNA, Recombinant Escherichia coli Proteins Hemolysin Proteins Hlya protein, E coli DNA Restriction Enzymes Serine Endopeptidases Endopeptidase K
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Felmlee T
Department of Medical Microbiology, University of Wisconsin Medical School, Madison 53706.
Welch R A
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.85.14.5269
Published
1988-07-00
Pages
5269-73
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC281731
Subset
IM
Grants
NIDDK NIH HHS · R01 DK063250 · United States
NIAID NIH HHS · AI20323 · United States
External Links
PubMed source DOI: 10.1073/pnas.85.14.5269 PMC Full Text View journal details
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