Imaging of fluorescence anisotropy during photoswitching provides a simple readout for protein self-association.

Abstract:

:Monitoring of protein oligomerization has benefited greatly from Förster Resonance Energy Transfer (FRET) measurements. Although donors and acceptors are typically fluorescent molecules with different spectra, homo-FRET can occur between fluorescent molecules of the same type if the emission spectrum overlaps with the absorption spectrum. Here, we describe homo-FRET measurements by monitoring anisotropy changes in photoswitchable fluorescent proteins while photoswitching to the off state. These offer the capability to estimate anisotropy in the same specimen during homo-FRET as well as non-FRET conditions. We demonstrate photoswitching anisotropy FRET (psAFRET) with a number of test chimeras and example oligomeric complexes inside living cells. We also present an equation derived from FRET and anisotropy equations which converts anisotropy changes into a factor we call delta r FRET (drFRET). This is analogous to an energy transfer efficiency and allows experiments performed on a given homo-FRET pair to be more easily compared across different optical configurations.

journal_name

Nat Commun

journal_title

Nature communications

authors

Ojha N,Rainey KH,Patterson GH

doi

10.1038/s41467-019-13843-6

subject

Has Abstract

pub_date

2020-01-07 00:00:00

pages

21

issue

1

issn

2041-1723

pii

10.1038/s41467-019-13843-6

journal_volume

11

pub_type

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