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A heterologous membrane protein domain fused to the C-terminal ATP-binding domain of HlyB can export Escherichia coli hemolysin.

The hydrophobic-rich NH2-terminal 34 amino acids of a tetracycline resistance determinant (TetC) were fused to the COOH-terminal 240 amino acids of the hemolysin transporter, HlyB, which contains a putative ATP-binding domain. This hybrid protein replaced the NH2-terminal 467-amino-acid portion of H...

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Bibliografische gegevens
Gepubliceerd in:J Bacteriol
Hoofdauteurs: Thomas, W D, Wagner, S P, Welch, R A
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: American Society for Microbiology (ASM) 1992
Onderwerpen:
Online toegang:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC207352/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1400227/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.174.21.6771-6779.1992
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