Issue 9, 2019
From the journal:

Chemical Communications

Light-control of the ultra-fast Gp41-1 split intein with preserved stability of a genetically encoded photo-caged amino acid in bacterial cells†

Jana K. Böcker,a   Wolfgang Dörnera  and  Henning D. Mootz ORCID logo *a  

* Corresponding authors

a Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Str. 2, D-48149 Münster, Germany
E-mail: Henning.Mootz@uni-muenster.de

Abstract

Inteins change the structure and function of their host protein in a unique way and the Gp41-1 split intein is the fastest protein trans-splicing intein known to date. To design a photo-activatable variant, we have incorporated ortho-nitrobenzyl-tyrosine (ONBY) at the position of a structurally conserved phenylalanine in the Gp41-1-N fragment. Using irradiation at 365 nm, the splicing reaction was triggered with virtually unchanged rates. The partial cellular reduction of the nitro group in ONBY, previously observed during bacterial protein expression for several photo-caged amino acids, was overcome by periplasmatic expression and by using an E. coli K12(DE3) strain instead of BL21(DE3). Together, our findings provide new tools for the artificial photo-control of proteins.

Graphical abstract: Light-control of the ultra-fast Gp41-1 split intein with preserved stability of a genetically encoded photo-caged amino acid in bacterial cells

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Article information

DOI
https://doi.org/10.1039/C8CC09204D
Article type
Communication
Submitted
19 Nov 2018
Accepted
04 Jan 2019
First published
07 Jan 2019

Chem. Commun., 2019,55, 1287-1290

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Light-control of the ultra-fast Gp41-1 split intein with preserved stability of a genetically encoded photo-caged amino acid in bacterial cells

J. K. Böcker, W. Dörner and H. D. Mootz, Chem. Commun., 2019, 55, 1287 DOI: 10.1039/C8CC09204D

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