β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions

Nature Biotechnology

Volumn 20, Issue 6, 2002, Pages 619-622

  Galarneau, André ^a   Primeau, Martin ^a   Trudeau, Louis Eric ^a   Michnick, Stephen W ^a  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BAD PROTEIN, HUMAN; BETA LACTAMASE; BETA LACTAMASE TEM 1; BETA-LACTAMASE TEM-1; CARRIER PROTEIN; CEPHALOSPORIN DERIVATIVE; DNA BINDING PROTEIN; FRAP1 PROTEIN, HUMAN; HYBRID PROTEIN; IMMUNOPHILIN; LEUCINE; NITROCEFIN; PEPTIDE FRAGMENT; PEPTIDE LIBRARY; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN BAD; PROTEIN BCL 2; PROTEIN KINASE; PROTEIN KINASE B KINASE; PROTEIN SERINE THREONINE KINASE; SACCHAROMYCES CEREVISIAE PROTEIN; SMAD3 PROTEIN; SMAD3 PROTEIN, HUMAN; TRANSACTIVATOR PROTEIN; RAPAMYCIN;

ANIMAL; ARTICLE; CATTLE; CELL LINE; CHEMISTRY; CYTOLOGY; FLUORESCENCE MICROSCOPY; GENETICS; HUMAN; INSTRUMENTATION; KIDNEY; METABOLISM; METHODOLOGY; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; REPRODUCIBILITY; SENSITIVITY AND SPECIFICITY; VALIDATION STUDY; COLORIMETRY; DIMERIZATION; DISSOCIATION CONSTANT; FLUORESCENCE; GENETIC COMPLEMENTATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; QUANTITATIVE ANALYSIS;

ANIMALS; BCL-ASSOCIATED DEATH PROTEIN; BETA-LACTAMASES; CARRIER PROTEINS; CATTLE; CELL LINE; CEPHALOSPORINS; DNA-BINDING PROTEINS; HUMANS; IMMUNOPHILINS; KIDNEY; LEUCINE; MICROSCOPY, FLUORESCENCE; PEPTIDE FRAGMENTS; PEPTIDE LIBRARY; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION MAPPING; PROTEIN KINASES; PROTEIN-SERINE-THREONINE KINASES; PROTEINS; PROTO-ONCOGENE PROTEINS C-BCL-2; RECOMBINANT FUSION PROTEINS; REPRODUCIBILITY OF RESULTS; SACCHAROMYCES CEREVISIAE PROTEINS; SENSITIVITY AND SPECIFICITY; SMAD3 PROTEIN; TRANS-ACTIVATORS; ANIMAL; HUMAN; SUPPORT, NON-U.S. GOV'T;

ASSAYS; CALORIMETRY; DIMERIZATION; ENZYMES; FLUORESCENCE; PROTEINS; SENSORS; SUBSTRATES; YEAST;

SIGNAL-TO-BACKGROUND RATIOS;

BIOTECHNOLOGY;

EID: 0035984722     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0602-619     Document Type: Article

References (20)

1. An in vivo library-versus-library selection of optimized protein-protein interactions
2. Clonal selection and in vivo quantitation of protein interactions with protein-fragment complementation assays
3. Erythropoietin receptor activation by a ligand-induced conformation change
4. Visualization of biochemical networks in living cells
5. Direct visualization of protein interactions in plant cells
6. Quantitation of transcription and clonal selection of single living cells with β-lactamase as reporter
7. Detection of protein-protein interactions by protein fragment complementation strategies
8. Oligomerization domaindirected reassembly of active dihydrofolate reductase from rationally designed fragments
9. Catalytic properties of class A β-lactamases: Efficiency and diversity
10. The diversity, structure and regulation of β-lactamases
11. Pentapeptide scanning mutagenesis: Random insertion of a variable five amino acid cassette in a target protein
12. Circularly permuted β-lactamase from Staphylococcus aureus PC 1
13. A natural polymorphism in β-lactamase is a global suppressor
14. A secondary drug resistance mutation of TEM-1 β-lactamase that suppresses misfolding and aggregation
15. Structure of Bcl-xL-Bak peptide complex: Recognition between regulators of apoptosis
16. Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue
17. Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
18. Monitoring protein-protein interactions in intact eukaryotic cells by β-galactosidase complementation
19. A genome-wide functional assay of signal transduction in living mammalian cells
20. Crystal structure of an acylation transition-state analog of the TEM-1 β-lactamase. Mechanistic implications for class A β-lactamases