DOI: 10.1146/annurev.biochem.70.1.39. DNA Primases

DNA Primases

10.1146/annurev.biochem.70.1.39

Crossref journal-article

Annual Reviews

Annual Review of Biochemistry (22)

Abstract

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

Bibliography

Frick, D. N., & Richardson, C. C. (2001). DNA Primases. Annual Review of Biochemistry, 70(1), 39â80.

Authors 2

David N. Frick (first)
Charles C. Richardson (additional)

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Dates

Type	When
Created	23 years, 1 month ago (July 27, 2002, 7:42 a.m.)
Deposited	3 years, 11 months ago (Oct. 5, 2021, 5:48 a.m.)
Indexed	5 days, 16 hours ago (Aug. 31, 2025, 6:22 a.m.)
Issued	24 years, 3 months ago (June 1, 2001)
Published	24 years, 3 months ago (June 1, 2001)
Published Print	24 years, 3 months ago (June 1, 2001)

Funders 0

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BibTeX

@article{Frick_2001, title={DNA Primases}, volume={70}, ISSN={1545-4509}, url={http://dx.doi.org/10.1146/annurev.biochem.70.1.39}, DOI={10.1146/annurev.biochem.70.1.39}, number={1}, journal={Annual Review of Biochemistry}, publisher={Annual Reviews}, author={Frick, David N. and Richardson, Charles C.}, year={2001}, month=jun, pages={39–80} }

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  "abstract": "<jats:p> \u25aa Abstract\u2002 DNA primases are enzymes whose continual activity is required at the DNA replication fork. They catalyze the synthesis of short RNA molecules used as primers for DNA polymerases. Primers are synthesized from ribonucleoside triphosphates and are four to fifteen nucleotides long. Most DNA primases can be divided into two classes. The first class contains bacterial and bacteriophage enzymes found associated with replicative DNA helicases. These prokaryotic primases contain three distinct domains: an amino terminal domain with a zinc ribbon motif involved in binding template DNA, a middle RNA polymerase domain, and a carboxyl-terminal region that either is itself a DNA helicase or interacts with a DNA helicase. The second major primase class comprises heterodimeric eukaryotic primases that form a complex with DNA polymerase alpha and its accessory B subunit. The small eukaryotic primase subunit contains the active site for RNA synthesis, and its activity correlates with DNA replication during the cell cycle. </jats:p>",
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