Primase

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Primase is the enzyme that synthesizes RNA primers, oligonucleotides that are complementarily bound to a nucleic acid polymer. Primase is required because DNA polymerases cannot initiate polymer synthesis on single-stranded DNA templates; they can only elongate from the 3'-hydroxyl of a primer. Primases fall into two major sequence and structure families: bacterial and archaeal/eukaryotic nuclear. Bacterial primases are monomers consisting of three domains. The N-terminal domain has a zinc-finger motif and is likely responsible for the initiation specificity of this enzyme. The central catalytic domain binds single-stranded DNA and catalyzes RNA polymer initiation and elongation complementary to it. The C-terminal domain interacts with other proteins, including DnaB helicase so that its activity takes place at the replication fork. The bacterial primase gene, dnaG, is the central gene of the macromolecular synthesis operon carrying the genes for the initiation phases of translation, replication, and transcription. Of the three genes, dnaG is under the most levels of control and is expressed in the lowest amount. Archaeal/eukaryotic primase resides in a heterotetramer consisting of a small primase subunit, a large primase subunit, a regulatory phosphoprotein, and DNA polymerase alpha. The small subunit has primer synthesis activity that is modulated by the other three proteins in the complex as well as by Replication protein A, a single-stranded DNA-binding protein required for lagging strand DNA synthesis, and the GINS complex, the central hub around which the leading- and lagging-strand DNA replicases assemble to control the progression of the replication fork. GINS interacts with the MCM helicase that translocates on the leading-strand template and also interacts with the DNA polymerase alpha/primase complex on the lagging strand.

Original languageEnglish (US)
Title of host publicationBrenner's Encyclopedia of Genetics
Subtitle of host publicationSecond Edition
PublisherElsevier Inc.
Pages450-453
Number of pages4
ISBN (Electronic)9780080961569
ISBN (Print)9780123749840
DOIs
StatePublished - Feb 27 2013

Fingerprint

DNA Primase
single-stranded DNA
DNA-directed DNA polymerase
polymers
synthesis
genes
Genes
RNA
family structure
Polymers
phosphoproteins
DNA-binding proteins
proteins
Single-Stranded DNA
zinc finger motif
DNA primers
DNA
operon
enzymes
active sites

Keywords

  • Codon usage bias
  • DNA ligase
  • DNA polymerase
  • DNA-strand break-sensitive ADP-ribosylation enzyme
  • DnaB helicase
  • DnaG
  • Fast-arrest replication phenotype
  • FEN-1 primer-removing nuclease
  • GINS
  • Heat-shock promoter
  • Macromolecular synthesis operon
  • MCM helicase
  • Nut antiterminator sequence
  • Okazaki fragment
  • PARP
  • Partition defect
  • Primase
  • Primer RNA
  • Replication protein A
  • Rho-independent terminator
  • RNase E
  • S21 ribosomal protein
  • Shine-Dalgarno sequence
  • Sigma subunit of RNA polymerase
  • Slow-arrest replication phenotype
  • Temperature-sensitive mutant
  • Twinkle

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Griep, M. A. (2013). Primase. In Brenner's Encyclopedia of Genetics: Second Edition (pp. 450-453). Elsevier Inc.. https://doi.org/10.1016/B978-0-12-374984-0.01208-0

Primase. / Griep, Mark A.

Brenner's Encyclopedia of Genetics: Second Edition. Elsevier Inc., 2013. p. 450-453.

Research output: Chapter in Book/Report/Conference proceedingChapter

Griep, MA 2013, Primase. in Brenner's Encyclopedia of Genetics: Second Edition. Elsevier Inc., pp. 450-453. https://doi.org/10.1016/B978-0-12-374984-0.01208-0
Griep MA. Primase. In Brenner's Encyclopedia of Genetics: Second Edition. Elsevier Inc. 2013. p. 450-453 https://doi.org/10.1016/B978-0-12-374984-0.01208-0
Griep, Mark A. / Primase. Brenner's Encyclopedia of Genetics: Second Edition. Elsevier Inc., 2013. pp. 450-453
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AB - Primase is the enzyme that synthesizes RNA primers, oligonucleotides that are complementarily bound to a nucleic acid polymer. Primase is required because DNA polymerases cannot initiate polymer synthesis on single-stranded DNA templates; they can only elongate from the 3'-hydroxyl of a primer. Primases fall into two major sequence and structure families: bacterial and archaeal/eukaryotic nuclear. Bacterial primases are monomers consisting of three domains. The N-terminal domain has a zinc-finger motif and is likely responsible for the initiation specificity of this enzyme. The central catalytic domain binds single-stranded DNA and catalyzes RNA polymer initiation and elongation complementary to it. The C-terminal domain interacts with other proteins, including DnaB helicase so that its activity takes place at the replication fork. The bacterial primase gene, dnaG, is the central gene of the macromolecular synthesis operon carrying the genes for the initiation phases of translation, replication, and transcription. Of the three genes, dnaG is under the most levels of control and is expressed in the lowest amount. Archaeal/eukaryotic primase resides in a heterotetramer consisting of a small primase subunit, a large primase subunit, a regulatory phosphoprotein, and DNA polymerase alpha. The small subunit has primer synthesis activity that is modulated by the other three proteins in the complex as well as by Replication protein A, a single-stranded DNA-binding protein required for lagging strand DNA synthesis, and the GINS complex, the central hub around which the leading- and lagging-strand DNA replicases assemble to control the progression of the replication fork. GINS interacts with the MCM helicase that translocates on the leading-strand template and also interacts with the DNA polymerase alpha/primase complex on the lagging strand.

KW - Codon usage bias

KW - DNA ligase

KW - DNA polymerase

KW - DNA-strand break-sensitive ADP-ribosylation enzyme

KW - DnaB helicase

KW - DnaG

KW - Fast-arrest replication phenotype

KW - FEN-1 primer-removing nuclease

KW - GINS

KW - Heat-shock promoter

KW - Macromolecular synthesis operon

KW - MCM helicase

KW - Nut antiterminator sequence

KW - Okazaki fragment

KW - PARP

KW - Partition defect

KW - Primase

KW - Primer RNA

KW - Replication protein A

KW - Rho-independent terminator

KW - RNase E

KW - S21 ribosomal protein

KW - Shine-Dalgarno sequence

KW - Sigma subunit of RNA polymerase

KW - Slow-arrest replication phenotype

KW - Temperature-sensitive mutant

KW - Twinkle

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BT - Brenner's Encyclopedia of Genetics

PB - Elsevier Inc.

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