DNA primases are enzymes whose continual activity is required at the DNA re
plication fork. They catalyze the synthesis of short RNA molecules used as
primers for DNA polymerases. Primers are synthesized from ribonucleoside tr
iphosphates and are four to fifteen nucleotides long. Most DNA primases can
be divided into two classes. The first class contains bacterial and bacter
iophage enzymes found associated with replicative DNA helicases. These prok
aryotic primases contain three distinct domains: an amino terminal domain w
ith a zinc ribbon motif involved in binding template DNA, a middle RNA poly
merase domain, and a carboxyl-terminal region that either is itself a DNA h
elicase or interacts with a DNA helicase. The second major primase class co
mprises heterodimeric eukaryotic primases that form a complex with DNA poly
merase alpha and its accessory B subunit. The small eukaryotic primase subu
nit contains the active site for RNA synthesis, and its activity correlates
with DNA replication during the cell cycle.