Multicolor Protein Labeling in Living Cells Using Mutant β-Lactamase-Tag Technology

2010 ◽  
Vol 21 (12) ◽  
pp. 2320-2326 ◽  
Author(s):  
Shuji Watanabe ◽  
Shin Mizukami ◽  
Yuichiro Hori ◽  
Kazuya Kikuchi
2010 ◽  
Vol 132 (12) ◽  
pp. 4455-4465 ◽  
Author(s):  
Duangkhae Srikun ◽  
Aaron E. Albers ◽  
Christine I. Nam ◽  
Anthony T. Iavarone ◽  
Christopher J. Chang

2021 ◽  
Author(s):  
Mullapudi Mohan Reddy ◽  
Punita Bathla ◽  
Britto S. Sandanaraj

AbstractSelf-assembly of a monomeric protease to form a multi-subunit protein complex “proteasome” enables targeted protein degradation in living cells. The naturally occurring proteasomes serve as an inspiration and blueprint for the design of artificial protein-based nanoreactors. Here we disclose a general chemical strategy for the design of proteasome-like nanoreactors. Micelle-assisted protein labeling (MAPLab) technology along with the N-terminal bioconjugation strategy is utilized for the synthesis of a well-defined monodisperse self-assembling semi-synthetic protease. The designer protein is programmed to self-assemble into a proteasome-like nanostructure which preserves the functional properties of native protease.


2015 ◽  
Vol 6 (5) ◽  
pp. 3217-3224 ◽  
Author(s):  
Yousuke Takaoka ◽  
Yuki Nishikawa ◽  
Yuki Hashimoto ◽  
Kenta Sasaki ◽  
Itaru Hamachi

A rapid and selective protein labeling method, LDBB chemistry is a useful tool for natural protein imaging in living cells.


2016 ◽  
Vol 52 (34) ◽  
pp. 5828-5831 ◽  
Author(s):  
Hankum Park ◽  
Ja Young Koo ◽  
Yellamelli V. V. Srikanth ◽  
Sangmi Oh ◽  
Jiyoon Lee ◽  
...  

The molecular shape of photoaffinity linkers significantly influences their nonspecific protein labeling of the cellular proteome.


2019 ◽  
Author(s):  
Zefan Li

Organelle specific protein identification is essential for understanding how cell functions in subcellular level. Here, we report a light mediated proximal labeling (LIMPLA) strategy for organelle specific protein profiling in living cells. In this strategy, various commercial mitochondria fluorescent trackers, such as Mitoview 405 and Rhodamine 123, can activate 2-Propynylamine (PA) to label proximal proteins in mitochondria under illumination. PA tagged proteins with alkynyl group are subsequently derivatized via click chemistry with azido fluorescent dye for imaging or with azido biotin for further enrichment and mass-spec identification. This strategy can be generalized to other organelles specific protein labeling. For example, proteins in nucleus are labeled by utilizing the commercial nucleus tracker DRAQ5. As compared with other chemical strategies for subcellular protein labeling, there are several advantages for this LIMPLA strategy. Target cells are no need of introducing of exogenous gene and some special treatments such as hydrogen peroxide or serum starvation, which ensure the minimal interference to cells status. All reagents used in this strategy are commercial available without additional synthesis work. Further, this strategy holds the potential for analyzing proximal proteins of specific macromolecules that can be tagged with fluorescent dye by metabolic labeling strategy.


2011 ◽  
Vol 15 (6) ◽  
pp. 768-774 ◽  
Author(s):  
Gražvydas Lukinavičius ◽  
Kai Johnsson

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