Issue 20, 2016

Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions

Abstract

We evaluate the ability of hexahistidine (His6) tags on peptide and protein substrates to recruit deoxyribozymes for modifying those substrates. For two different deoxyribozymes, one that creates tyrosine-RNA nucleopeptides and another that phosphorylates tyrosine side chains, we find substantial improvements in yield, kobs, and Km for peptide substrates due to recruiting by His6/Cu2+. However, the recruiting benefits of the histidine tag are not observed for larger protein substrates, likely because the tested deoxyribozymes either cannot access the target peptide segments or cannot function when these segments are presented in a structured protein context.

Graphical abstract: Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions

Supplementary files

Article information

Article type
Paper
Submitted
06 Apr 2016
Accepted
27 Apr 2016
First published
27 Apr 2016
This article is Open Access
Creative Commons BY license

Org. Biomol. Chem., 2016,14, 4697-4703

Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions

C. Chu and S. K. Silverman, Org. Biomol. Chem., 2016, 14, 4697 DOI: 10.1039/C6OB00716C

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