Archaeal and eukaryote primases are heterodimeric proteins with one large regulatory and one minuscule catalytic subunit.
[4] The central subdomain forms a toprim fold which is made of a mixture five beta sheets and six alpha helices.
[12] This classification also emphasizes the broad origins of AEP primases; the superfamily is now recognized as transitioning between RNA and DNA functions.
For example, removing the part corresponding to the large subunit in a fusion protein PolpTN2 results in a slower enzyme with reverse transcriptase activity.
[16][11] Primases with terminal transferase functionality are capable of adding nucleotides to the 3’ end of a DNA strand independently of a template.
[17] Human PrimPol (ccdc111[16]) serves both primase and polymerase functions, like many archaeal primases; exhibits terminal transferase activity in the presence of manganese; and plays a significant role in translesion synthesis[18] and in restarting stalled replication forks.
PrimPol is actively recruited to damaged sites through its interaction with RPA, an adapter protein that facilitates DNA replication and repair.
[18] Unlike most primases, PrimPol is uniquely capable of starting DNA chains with dNTPs.
[16] PriS, the archaeal primase small subunit, has a role in translesion synthesis (TLS) and can bypass common DNA lesions.
[19] PriS alone preferentially synthesizes strings of DNA; but in combination with PriL, the large subunit, RNA polymerase activity is increased.
[21] AEP enzymes are widespread, and can be found encoded in mobile genetic elements including virus/phages and plasmids.
[14] A great diversity of AEP families has been uncovered in various bacterial plasmids by comparative genomics surveys.
[14] Their evolutionary history is currently unknown, as these found in bacteria and bacteriophages appear too different from their archaeo-eukaryotic homologs for a recent horizontal gene transfer.
A fusion of domains homologous to PriS and PriL, it exhibits both primase and DNA polymerase activity, as well as terminal transferase function.