The deoxyribo-mode expression of primase activities of the primase-alpha DNA polymerase enzyme complex associated with nucleoprotein complexes harboring an extrachromosomal DNA identical with avian myeloblastosis virus core-bound DNA: influencing by carbonyldiphosphonate, mimosine and butylphenyl deoxyguanosine-5'-triphosphate.

The deoxyribo-mode expression of primase (Pr) activities of the Pr-alpha DNA polymerase (pol) enzyme complex belonging to the naturally occurring nucleoprotein (NP) complexes harboring an extrachromosomal DNA identical with avian myeloblastosis virus (AMV) core-bound DNA (Riman and Sulova, Acta Virol. 41, 181-192 (1997)) is similarly influenced by carbonyldiphosphonate (COMDP) as the ribo-mode expression of Pr activities (Riman, Acta Virol. 45, 109-124 (2001)). In the presence of all four common dNTPs only and dNTPs and rNTPs in the reaction medium, COMDP strongly activates the deoxyribo-mode of Pr activities and again induces a unique phenomenon of primer accumulation. These primers labeled for DNA are up to 90% alkali-resistant and sensitive to DNase I treatment. This suggests that they are constituted mostly of deoxynucleotides (dnts). In contrast to the stimulation of the ribo-mode expression of Pr activities by COMDP, the incorporated radioactivity is in this case more than one order lesser. 1-Mimosine-(alpha-amino-beta-[N-(3-hydroxy-4-pyridone)]-propionic acid (MIMO) is again able to substantially eliminate the phenomenon of primer accumulation, suggesting that also in this case the effects of COMDP and MIMO are, at certain reaction conditions, mutually exclusive and that both agents compete for the same active site responsible for mutual coupling of Pr and alpha DNA pol activities.