期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 135, 期 40, 页码 14928-14931出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja407586u
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资金
- National Institutes of Health [R01GM065966]
- Defense Threat Reduction Agency [HDTRAI-09-1-0011]
- National Science Foundation [CHE0842534]
- NIH [T32 GM070421]
We show that DNA catalysts (deoxyribozymes, DNA enzymes) can phosphorylate tyrosine residues of peptides. Using in vitro selection, we identified deoxyribozymes that transfer the gamma-phosphoryl group from a 5'-triphosphorylated donor (a pppRNA oligonucleotide or GTP) to the tyrosine hydroxyl acceptor of a tethered hexapeptide. Tyrosine kinase deoxyribozymes that use pppRNA were identified from each of N-30, N-40, and N-50 random-sequence pools. Each deoxyribozyme requires Zn2+, and most additionally require Mn2+. The deoxyribozymes have little or no selectivity for the amino acid identities near the tyrosine, but they are highly selective for phosphorylating tyrosine rather than serine. Analogous GTP-dependent DNA catalysts were identified and found to have apparent K-m(GTP) as low as similar to 20 mu M. These findings establish that DNA has the fundamental catalytic ability to phosphorylate the tyrosine side chain of a peptide substrate.
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