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Versatile and Efficient Site-Specific Protein Functionalization by Tubulin Tyrosine Ligase.

Schumacher, Dominik ; Helma, Jonas ; Mann, Florian A. ; Pichler, Garwin ; Natale, Francesco ; Krause, Eberhard ; Cardoso, M. Cristina ; Hackenberger, Christian P. R. ; Leonhardt, Heinrich (2015):
Versatile and Efficient Site-Specific Protein Functionalization by Tubulin Tyrosine Ligase.
In: Angewandte Chemie (International ed. in English), 54 (46), pp. 13787-13791. ISSN 1521-3773,
[Article]

Abstract

A novel chemoenzymatic approach for simple and fast site-specific protein labeling is reported. Recombinant tubulin tyrosine ligase (TTL) was repurposed to attach various unnatural tyrosine derivatives as small bioorthogonal handles to proteins containing a short tubulin-derived recognition sequence (Tub-tag). This novel strategy enables a broad range of high-yielding and fast chemoselective C-terminal protein modifications on isolated proteins or in cell lysates for applications in biochemistry, cell biology, and beyond, as demonstrated by the site-specific labeling of nanobodies, GFP, and ubiquitin.

Item Type: Article
Erschienen: 2015
Creators: Schumacher, Dominik ; Helma, Jonas ; Mann, Florian A. ; Pichler, Garwin ; Natale, Francesco ; Krause, Eberhard ; Cardoso, M. Cristina ; Hackenberger, Christian P. R. ; Leonhardt, Heinrich
Title: Versatile and Efficient Site-Specific Protein Functionalization by Tubulin Tyrosine Ligase.
Language: English
Abstract:

A novel chemoenzymatic approach for simple and fast site-specific protein labeling is reported. Recombinant tubulin tyrosine ligase (TTL) was repurposed to attach various unnatural tyrosine derivatives as small bioorthogonal handles to proteins containing a short tubulin-derived recognition sequence (Tub-tag). This novel strategy enables a broad range of high-yielding and fast chemoselective C-terminal protein modifications on isolated proteins or in cell lysates for applications in biochemistry, cell biology, and beyond, as demonstrated by the site-specific labeling of nanobodies, GFP, and ubiquitin.

Journal or Publication Title: Angewandte Chemie (International ed. in English)
Journal volume: 54
Number: 46
Divisions: 10 Department of Biology
10 Department of Biology > Cell Biology and Epigenetics
Date Deposited: 01 Oct 2015 06:29
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