EC Number   |
General Information |
Reference |
|---|
   2.7.7.B17 | evolution |
PolpTN2 is indeed formed by the association of an N-terminal DNA polymerase/primase domain and a C-terminal domain whose sequences bear a distant similarity to the catalytic and regulatory subunits, respectively, of heterodimeric (PriS-PriL) archaeal and eukaryotic primases. The N-terminal domain possesses reverse transcriptase activity this activity can reflect an ancestral function of archaeal and eukaryotic primases proteins in the transition from the RNA to the DNA world |
739194 |
| 2.7.7.B17 | malfunction |
plasmids lacking orf904 and orf56 but harboring the putative origin are transformable when orf904 and orf56 are provided in-trans, a 75-bp region 5' of the orf904 start codon is essential for the complementation |
-, 739492 |
| 2.7.7.B17 | more |
the loop of the 100-bp structure of the 232-bp region of plasmid pRN1 contains a GTG tri-nucleotide motif, a feature that is important for the primase activity of Orf904. This putative origin and the associated orf56 and orf904 are identified as the minimal replicon of pRN1 |
-, 739492 |
| 2.7.7.B17 | physiological function |
PolpTN2 exhibits DNA polymerase, DNA primase and nucleotidyl terminal transferase activities. PolpTN2 can efficiently prime DNA synthesis by cellular DNA polymerases, suggesting that this protein is used in vivo as primase for pTN2 plasmid replication. The PriL-like domain enhances the stringency of PolpTN2 polymerase. The N-terminal PriS-like domain of PolpTN2 exhibits all activities of the full-length enzyme but is much less efficient in priming cellular DNA polymerases. The N-terminal domain possesses reverse transcriptase activity |
739194 |
