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

Chih Chi Chu, Scott K Silverman

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)4697-4703
Number of pages7
JournalOrganic and Biomolecular Chemistry
Volume14
Issue number20
DOIs
StatePublished - Jan 1 2016

Fingerprint

His-His-His-His-His-His
Catalytic DNA
histidine
Histidine
peptides
proteins
Peptides
Tyrosine
tyrosine
Substrates
Proteins
RNA

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

Cite this

Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions. / Chu, Chih Chi; Silverman, Scott K.

In: Organic and Biomolecular Chemistry, Vol. 14, No. 20, 01.01.2016, p. 4697-4703.

Research output: Contribution to journalArticle

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