scholarly journals A straightforward approach for bioorthogonal labeling of proteins and organelles in live mammalian cells, using a short peptide tag

2019 ◽  
Author(s):  
Inbar Segal ◽  
Dikla Nachmias ◽  
Eyal Arbely ◽  
Natalie Elia

AbstractIn the high-resolution microscopy era, genetic code expansion (GCE)-based bioorthogonal labeling offers an elegant way for direct labeling of proteins in live cells with fluorescent dyes. This labeling approach is currently not broadly used live cell applications, partly because it needs to be adjusted to the specific protein under study. Here, we present a generic, 14-residues long, N-terminal tag for GCE-based labeling of proteins in live mammalian cells. Using this tag, we generated a library of GCE-based organelle markers, demonstrating the applicability of the tag for labeling a plethora of proteins and organelles. Finally, we show that the HA epitope, used as a backbone in our tag, can be substituted with other epitopes and, in some cases, can be completely removed, reducing the tag length to 5 residues. The GCE-tag presented here offers a powerful, easy-to-implement tool for live cell labeling of cellular proteins with small and bright probes.

2017 ◽  
Vol 28 (21) ◽  
pp. 2747-2756 ◽  
Author(s):  
Tomer Schvartz ◽  
Noa Aloush ◽  
Inna Goliand ◽  
Inbar Segal ◽  
Dikla Nachmias ◽  
...  

Genetic code expansion and bioorthogonal labeling provide for the first time a way for direct, site-specific labeling of proteins with fluorescent-dyes in live cells. Although the small size and superb photophysical parameters of fluorescent-dyes offer unique advantages for high-resolution microscopy, this approach has yet to be embraced as a tool in live cell imaging. Here we evaluated the feasibility of this approach by applying it for α-tubulin labeling. After a series of calibrations, we site-specifically labeled α-tubulin with silicon rhodamine (SiR) in live mammalian cells in an efficient and robust manner. SiR-labeled tubulin successfully incorporated into endogenous microtubules at high density, enabling video recording of microtubule dynamics in interphase and mitotic cells. Applying this labeling approach to structured illumination microscopy resulted in an increase in resolution, highlighting the advantages in using a smaller, brighter tag. Therefore, using our optimized assay, genetic code expansion provides an attractive tool for labeling proteins with a minimal, bright tag in quantitative high-resolution imaging.


2017 ◽  
Vol 23 (50) ◽  
pp. 12114-12119 ◽  
Author(s):  
Alexey N. Butkevich ◽  
Vladimir N. Belov ◽  
Kirill Kolmakov ◽  
Viktor V. Sokolov ◽  
Heydar Shojaei ◽  
...  

2015 ◽  
Vol 137 (33) ◽  
pp. 10452-10455 ◽  
Author(s):  
Peter V. Robinson ◽  
Gabriela de Almeida-Escobedo ◽  
Amber E. de Groot ◽  
Julia L. McKechnie ◽  
Carolyn R. Bertozzi

2015 ◽  
Vol 51 (23) ◽  
pp. 4895-4898 ◽  
Author(s):  
Cecilia Samaniego Lopez ◽  
María Amparo Lago Huvelle ◽  
María Laura Uhrig ◽  
Federico Coluccio Leskow ◽  
Carla C. Spagnuolo

The detection performance in solution and in live cells of a novel mono-boronic acid derivative of a near-infrared luminescent tricarbocyanine with OFF–ON response upon addition of saccharides.


2015 ◽  
Vol 21 (35) ◽  
pp. n/a-n/a
Author(s):  
Jan-Erik Hoffmann ◽  
Tilman Plass ◽  
Ivana Nikić ◽  
Iker Valle Aramburu ◽  
Christine Koehler ◽  
...  

PLoS ONE ◽  
2015 ◽  
Vol 10 (11) ◽  
pp. e0141918 ◽  
Author(s):  
Zhongqiu Ni ◽  
Lanxia Zhou ◽  
Xu Li ◽  
Jing Zhang ◽  
Shouliang Dong

2017 ◽  
Author(s):  
Noa Aloush ◽  
Tomer Schvartz ◽  
Andres I. König ◽  
Sarit Cohen ◽  
Eugene Brozgol ◽  
...  

ABSTRACTGenetic code expansion enables the incorporation of non-canonical amino acids (ncAAs) into expressed proteins. ncAAs are usually encoded by a stop codon that is decoded by an exogenous orthogonal aminoacyl tRNA synthetase and its cognate suppressor tRNA, such as the pyrrolysine synthetase/ pair. In such systems, stop codon suppression is dependent on the intracellular levels of the exogenous tRNA. Therefore, multiple copies of the tRNAPyl gene (PylT) are encoded to improve ncAA incorporation. However, certain applications in mammalian cells, such as live-cell imaging applications, where labelled tRNA contributes to background fluorescence, can benefit from the use of less invasive minimal expression systems. Accordingly, we studied the effect of tRNAPyl on live-cell fluorescence imaging of bioorthogonally-labelled intracellular proteins. We found that in COS7 cells, a decrease in PylT copy numbers had no measurable effect on protein expression levels. Importantly, reducing PylT copy numbers improved the quality of live-cells images by enhancing the signal-to-noise ratio and reducing an immobile tRNAPyl population. This enabled us to improve live cell imaging of bioorthogonally labelled intracellular proteins, and to simultaneously label two different proteins in a cell. Our results indicate that the number of introduced PylT genes can be minimized according to the transfected cell line, incorporated ncAA, and application.


2020 ◽  
Vol 2 (12) ◽  
pp. 5803-5809
Author(s):  
Lei Dong ◽  
Dehong Hu ◽  
Yanding Wang ◽  
Zonghai Sheng ◽  
Mei Hong ◽  
...  

The smallest-pore SAPO-20 zeolite confined pyrolysis of organics afforded ultrasmall uniform carbon dots with excellent performance in bioimaging.


2004 ◽  
Vol 16 (12) ◽  
pp. 961-966 ◽  
Author(s):  
A. M. Derfus ◽  
W. C. W. Chan ◽  
S. N. Bhatia

2010 ◽  
Vol 59 (3) ◽  
pp. 357-363 ◽  
Author(s):  
Ophélie Nicolle ◽  
Astrid Rouillon ◽  
Helene Guyodo ◽  
Zohreh Tamanai-Shacoori ◽  
Fatiha Chandad ◽  
...  

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