期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 38, 页码 11397-11402出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201605366
关键词
argpyrimidine; biological activity; chaperone proteins; protein modifications; protein semisynthesis
资金
- Austrian Academy of Sciences
- APART fellowship of the Austrian Academy of Sciences
Non-enzymatic posttranslational modifications (nPTMs) affect at least approximate to 30% of human proteins, but our understanding of their impact on protein structure and function is limited. Studies of nPTMs are difficult because many modifications are not included in common chemical libraries or protein expression systems and should be introduced site-specifically. Herein, we probed the effect of the nPTM argpyrimidine on the structure and function of human protein Hsp27, which acquires argpyrimidine at residue 188 invivo. We developed a synthetic approach to an argpyrimidine building block, which we then incorporated at position 188 of Hsp27 through protein semisynthesis. This modification did not affect the protein secondary structure, but perturbed the oligomeric assembly and impaired chaperone activity. Our work demonstrates that protein function can be altered by a single nPTM and opens up a new area of investigation only accessible by methods that allow site-selective protein modification.
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