Detection of protein interactions based on GFP fragment complementation by fluorescence microscopy and spectrofluorometry

Biotechniques. 2008 Jan;44(1):70, 72, 74. doi: 10.2144/000112685.

Abstract

We have developed a set of simple modifications of the green fluorescent protein (GFP)fragment reassembly assay in bacteria that permits: (i)fluorescent microscopy visualization of GFP reassembly only 1-2 h after induction of protein expression, thus approximating the detection of GFP reassembly to the real-time dynamics of protein complex formation in living cells; (ii) spectrofluorometric detection of reassembled GFP fluorescent signals directly in lysates from cell suspension thereby avoiding, in many cases, the need for tag-affinity isolation of protein complexes; and (iii) comparative quantification of signal intensity in numerous cell-sample lysates using a Bio-Rad IQ5 spectrofluorometric detection system (Bio-Rad Laboratories, Madrid, Spain). Collectively, the results demonstrate that the combination of microscopic and spectrofluorometric detection provides a time-saving and sensitive alternative to existing methods of fluorescence complementation analysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / cytology
  • Genetic Complementation Test*
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism*
  • Microscopy, Fluorescence / methods*
  • Peptide Fragments / metabolism*
  • Protein Binding
  • Protein Interaction Mapping
  • Spectrometry, Fluorescence / methods*

Substances

  • Peptide Fragments
  • Green Fluorescent Proteins