A thermostable d-polymerase for mirror-image PCR.

Abstract:

:Biological evolution resulted in a homochiral world in which nucleic acids consist exclusively of d-nucleotides and proteins made by ribosomal translation of l-amino acids. From the perspective of synthetic biology, however, particularly anabolic enzymes that could build the mirror-image counterparts of biological macromolecules such as l-DNA or l-RNA are lacking. Based on a convergent synthesis strategy, we have chemically produced and characterized a thermostable mirror-image polymerase that efficiently replicates and amplifies mirror-image (l)-DNA. This artificial enzyme, dubbed d-Dpo4-3C, is a mutant of Sulfolobus solfataricus DNA polymerase IV consisting of 352 d-amino acids. d-Dpo4-3C was reliably deployed in classical polymerase chain reactions (PCR) and it was used to assemble a first mirror-image gene coding for the protein Sso7d. We believe that this d-polymerase provides a valuable tool to further investigate the mysteries of biological (homo)chirality and to pave the way for potential novel life forms running on a mirror-image genome.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Pech A,Achenbach J,Jahnz M,Schülzchen S,Jarosch F,Bordusa F,Klussmann S

doi

10.1093/nar/gkx079

subject

Has Abstract

pub_date

2017-04-20 00:00:00

pages

3997-4005

issue

7

eissn

0305-1048

issn

1362-4962

pii

2966301

journal_volume

45

pub_type

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