A yeast sensor of ligand binding View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-11

AUTHORS

Chandra L. Tucker, Stanley Fields

ABSTRACT

We describe a biosensor that reports the binding of small-molecule ligands to proteins as changes in growth of temperature-sensitive yeast. The yeast strains lack dihydrofolate reductase (DHFR) and are complemented by mouse DHFR containing a ligand-binding domain inserted in a flexible loop. Yeast strains expressing two ligand-binding domain fusions, FKBP12-DHFR and estrogen receptor-α (ERα)-DHFR, show increased growth in the presence of their corresponding ligands. We used this sensor to identify mutations in residues of ERα important for ligand binding, as well as mutations generally affecting protein activity or expression. We also tested the sensor against a chemical array to identify ligands that bind to FKBP12 or ERα. The ERα sensor was able to discriminate among estrogen analogs, showing different degrees of growth for the analogs that correlated with their relative binding affinities (RBAs). This growth assay provides a simple and inexpensive method to select novel ligands and ligand-binding domains. More... »

PAGES

1042-1046

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nbt1101-1042

DOI

http://dx.doi.org/10.1038/nbt1101-1042

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1053677618

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11689849


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213 schema:name Departments of Genetics and Medicine, University of Washington, Box 357360, 98195, Seattle, WA
214 Howard Hughes Medical Institute, University of Washington, Box 357360, 98195, Seattle, WA
215 rdf:type schema:Organization
 




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