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Enhancing the biophysical properties of mRFP1 through incorporation of fluoroproline.

Abstract：

:Here we enhanced the stability and biophysical properties of mRFP1 through a combination of canonical and non-canonical amino acid mutagenesis. The global replacement of proline residue with (2S, 4R)-4-fluoroproline [(4R)-FP] into mRFP1 led to soluble protein but lost its fluorescence, whereas (2S, 4S)-4-fluoroproline [(4S)-FP] incorporation resulted in insoluble protein. The bioinformatics analysis revealed that (4R)-FP incorporation at Pro63 caused fluorescence loss due to the steric hindrance of fluorine atom of (4R)-FP with the chromophore. Therefore, Pro63 residue was mutated with the smallest amino acid Ala to maintain non coplanar conformation of the chromophore and helps to retain its fluorescence with (4R)-FP incorporation. The incorporation of (4R)-FP into mRFP1-P63A showed about 2-3-fold enhancement in thermal and chemical stability. The rate of maturation is also greatly accelerated over the presence of (4R)-FP into mRFP1-P63A. Our study showed that a successful enhancement in the biophysical property of mRFP1-P63A[(4R)-FP] using non-canonical amino acid mutagenesis after mutating non-permissive site Pro63 into Ala.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Deepankumar K,Nadarajan SP,Ayyadurai N,Yun H

doi

10.1016/j.bbrc.2013.09.062

subject

Has Abstract

pub_date

2013-11-01 00:00:00

pages

509-14

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(13)01543-X

journal_volume

440

pub_type

杂志文章

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