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© Institut Pasteur
Cristaux de cellulase, enzyme purifiée de Clostridium thermocellum permettant la digestion de la cellulose. Image colorisée.
Publication : Biochemistry

Enzymatic incorporation in DNA of 1,5-anhydrohexitol nucleotides

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemistry - 24 Oct 2000

Vastmans K, Pochet S, Peys A, Kerremans L, Van Aerschot A, Hendrix C, Marlière P, Herdewijn P

Link to Pubmed [PMID] – 11041840

Biochemistry 2000 Oct;39(42):12757-65

The ability of several DNA polymerases to catalyze the template-directed synthesis of duplex oligonucleotides containing a base pair between a nucleotide with anhydrohexitol ring and its natural complement has been investigated. All DNA polymerases were able to accept the chemically synthesized anhydrohexitol triphosphate as substrate and to catalyze the incorporation of one anhydrohexitol nucleotide. However, only family B DNA polymerases succeeded in elongating the primer after the incorporation of an anhydrohexitol nucleotide. In this family, Vent (exo(-)) DNA polymerase is the most successful one and was therefore selected for further investigation. Results revealed that at high enzyme concentrations six hATPs could be incorporated; however, a selective incorporation proved only feasible under experimental conditions where no more than two analogues could be inserted. Also the synthesis of a mixed HNA-DNA sequence was examined. Kinetic parameters for incorporation of one anhydrohexitol adenine nucleoside were similar to those of its natural analogue.

http://www.ncbi.nlm.nih.gov/pubmed/11041840