Unknown

Dataset Information

0

Cell surface β-lactamase recruitment: A facile selection to identify protein-protein interactions.


ABSTRACT: 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 β-lactamase recruitment on the surface of Escherichia coli with resistance to ampicillin. Bacteria displaying a protein that forms a complex with a specific protein-β-lactamase fusion are protected from ampicillin-dependent cell death. In contrast, bacteria that do not recruit β-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.

SUBMITTER: Hinmon JA 

PROVIDER: S-EPMC10949332 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Cell surface β-lactamase recruitment: A facile selection to identify protein-protein interactions.

Hinmon Jordan A JA   King Jade M JM   Mayo Latrina J LJ   Faries Cierra R CR   Lockett Ya'hnis T YT   Crawford David W DW   Beardslee Patrick C PC   Hendricks Alexander A   McNaughton Brian R BR  

Protein science : a publication of the Protein Society 20240401 4


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 β-lactamase recruitment on the surface of Escherichia coli with resistance to ampicillin. Bacteria displaying a protein that forms a complex with a spec  ...[more]

Similar Datasets

| S-EPMC3822001 | biostudies-literature
| S-EPMC4597145 | biostudies-literature
| S-EPMC9574477 | biostudies-literature
2022-02-28 | PXD002480 | Pride
| S-EPMC9137480 | biostudies-literature
| S-EPMC4838597 | biostudies-literature
| S-EPMC11129921 | biostudies-literature