The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Transport of hemolysin across the outer membrane of Escherichia coli requires two functions
Open accessAbstract
Among a large collection of hemolysis-negative mutants obtained by mutagenesis of the Hly plasmid pHly152 with Tn5, we have isolated two classes of mutants which are defective in the transport of hemolysin across the outer membrane. The two cistrons (hylBa and hlyBb) which are affected in these mutants are located adjacent to each other on the hly determinant but are transcribed from different promoters. Recombinant plasmids were constructed which carry the two functions as combined or separated cistrons. These were shown to complement the two types of transport mutants. Studies on the compartmentation of hemolysin in these two classes of mutants indicate that most hemolysin (greater than 70%) in hlyBa mutants is located in the periplasmic space, whereas in hlyBb mutants a larger portion of hemolysin is associated with the outer membrane fraction. The phenotypic appearance of colonies from hlyBb mutants is that of beta-hemolytic Escherichia coli strains, indicating that a substantial portion of hemolysin has already reached the outside of the outer membrane without being released into the medium. Release was achieved readily when hlyBb mutants were complemented with a recombinant plasmid carrying hlyBb.
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Cites
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Welch, R. A., Dellinger, E. P., Minshew, B., & Falkow, S. (1981) · Nature · doi:10.1038/294665a0 · Cited by 330
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Polarity of Tn5 insertion mutations in Escherichia coli
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Genetics of bacteriocins produced by lactic acid bacteria
Klaenhammer, T. (1993) · FEMS Microbiology Reviews · doi:10.1016/0168-6445(93)90057-g · Cited by 2,029
Virulence factors in Escherichia coli urinary tract infection
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RTX proteins: a highly diverse family secreted by a common mechanism
Linhartová, I., Bumba, L., Mašín, J., Basler, M., Osička, R., Kamanová, J., Procházková, K., Adkins, I., Hejnová-Holubová, J., Sadílková, L., et al. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00231.x · Cited by 530
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Structure and Function of TolC: The Bacterial Exit Duct for Proteins and Drugs
Koronakis, V., Eswaran, J., & Hughes, C. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074104 · Cited by 357
Metadata
- Authors
- Wagner, W., Vogel, M., & Goebel, W.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1983-04
- Volume
- 154
- Issue
- 1
- Pages
- 200-210
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- OpenAlex
- W2127557420
- Cited by
- 255
- References
- 15
- FWCI
- 12.20
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Wagner, W., Vogel, M., & Goebel, W. (1983). Transport of hemolysin across the outer membrane of Escherichia coli requires two functions. Journal of Bacteriology. https://doi.org/10.1128/jb.154.1.200-210.1983
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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