How cyanophage s-2l rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its dna

HIGHLIGHTS

• who: Dariusz Czernecki from the Institut have published the research work: How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its DNA, in the Journal: NATURE COMMUNICATIONS NATURE COMMUNICATIONS
• what: The authors confirm its polymerase activity but find that the enzyme is not specific to A or Z. Instead, the authors propose that the absence of A in S-2L genome is explained by a separate enzyme, an HD phosphohydrolase that specifically dephosphorylates dATP and that the authors name DatZ. Either D87 is able to come back to its . . .
  

   

  

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