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Post‐translational Assembly of Protein Parts into Complex Devices by Using SpyTag/SpyCatcher Protein Ligase
Author(s) -
Sutherland Ashley R.,
Alam Md. Kausar,
Geyer C. Ronald
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800538
Subject(s) - modularity (biology) , computational biology , protein engineering , posttranslational modification , ubiquitin ligase , template , synthetic biology , biology , computer science , nanotechnology , genetics , biochemistry , ubiquitin , enzyme , gene , programming language , materials science
Exploiting the innate modularity of proteins has allowed advances across the fields of synthetic biology and biotechnology. By using standardized protein components as building blocks, complex, multiprotein assemblies with sophisticated functions can be generated; feats previously not possible with strictly genetic‐engineering approaches. The development of strategies for protein assembly is accelerating, pushing the boundaries of protein architecture. SpyTag and SpyCatcher protein ligase is a recent advance in this field that allows plug‐and‐play modularity by harnessing post‐translational protein assembly. Herein, we review the latest applications of this powerful tool including novel enzyme assemblies, modularizing protein display, and the generation of antibody and antibody‐like “devices” by using SpyTag/SpyCatcher technology.

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