Journal
CELL DISCOVERY
Volume 3, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/celldisc.2017.37
Keywords
chirality; D-amino acid; L-DNA; mirror-image polymerase chain reaction (miPCR); Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4)
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Funding
- Ministry of Science and Technology of China [2015CB553402, 2016YFC0206300, 2017YFA0505200]
- National Natural Science Foundation of China [31470532, 91543102, 31711530153, 21532004]
- Beijing Nova Program [Z171100001117011]
- Tsinghua University Initiative Scientific Research Program [20161080152]
- Tsinghua University-Peking University Center for Life Sciences (CLS)
- Beijing Advanced Innovation Center for Structural Biology
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The construction of mirror-image biological systems may open the next frontier for biomedical technology development and discovery. Here we have designed and chemically synthesized a mutant version of the thermostable Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) consisting of D-amino acids. With a total peptide length of 358 amino acid residues, it is the largest chemically synthesized D-amino acid protein reported to date. We show that the D-polymerase is able to amplify a 120-bp L-DNA sequence coding for the Escherichia coli 5S ribosomal RNA gene rrfB by mirror-image polymerase chain reaction, and that both the natural and mirror-image systems operate with strict chiral specificity. The development of efficient miPCR systems may lead to many practical applications, such as mirror-image systematic evolution of ligands by exponential enrichment for the selection of therapeutically promising nuclease-resistant L-nucleic acid aptamers.
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