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Protein Sci ; 33(4): e4919, 2024 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-38501433

RESUMEN

Protein-protein interactions (PPIs) are central to many cellular processes, and the identification of novel PPIs is a critical step in the discovery of protein therapeutics. Simple methods to identify naturally existing or laboratory evolved PPIs are therefore valuable research tools. We have developed a facile selection that links PPI-dependent ß-lactamase recruitment on the surface of Escherichia coli with resistance to ampicillin. Bacteria displaying a protein that forms a complex with a specific protein-ß-lactamase fusion are protected from ampicillin-dependent cell death. In contrast, bacteria that do not recruit ß-lactamase to the cell surface are killed by ampicillin. Given its simplicity and tunability, we anticipate this selection will be a valuable addition to the palette of methods for illuminating and interrogating PPIs.


Asunto(s)
Ampicilina , beta-Lactamasas , beta-Lactamasas/genética , beta-Lactamasas/metabolismo , Ampicilina/farmacología , Ampicilina/metabolismo , Bacterias/metabolismo , Escherichia coli/genética , Escherichia coli/metabolismo , Membrana Celular/metabolismo , Antibacterianos/metabolismo
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