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A fluorescent variant of a protein from the stony coral Montipora facilitates dual-color single-laser fluorescence cross-correlation spectroscopy.

Abstract：

:Dual-color fluorescence cross-correlation spectroscopy (FCCS) is a promising technique for quantifying protein-protein interactions. In this technique, two different fluorescent labels are excited and detected simultaneously within a common measurement volume. Difficulties in aligning two laser lines and emission crossover between the two fluorophores, however, make this technique complex. To overcome these limitations, we developed a fluorescent protein with a large Stokes shift. This protein, named Keima, absorbs and emits light maximally at 440 nm and 620 nm, respectively. Combining a monomeric version of Keima with cyan fluorescent protein allowed dual-color FCCS with a single 458-nm laser line and complete separation of the fluorescent protein emissions. This FCCS approach enabled sensitive detection of proteolysis by caspase-3 and the association of calmodulin with calmodulin-dependent enzymes. In addition, Keima and a spectral variant that emits maximally at 570 nm might facilitate simultaneous multicolor imaging with single-wavelength excitation.

journal_name

Nat Biotechnol

journal_title

Nature biotechnology

authors

Kogure T,Karasawa S,Araki T,Saito K,Kinjo M,Miyawaki A

doi

10.1038/nbt1207

subject

Has Abstract

pub_date

2006-05-01 00:00:00

pages

577-81

issue

5

eissn

1087-0156

issn

1546-1696

pii

nbt1207

journal_volume

24

pub_type

杂志文章

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