DNA primases.

  title={DNA primases.},
  author={D. Frick and C. Richardson},
  journal={Annual review of biochemistry},
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… Expand
Properties of an unusual DNA primase from an archaeal plasmid
The primase activity of the replication protein from the archaeal plasmid pRN1 synthesizes a rather unusual mixed primer consisting of a single ribonucleotide at the 5′ end followed by seven deoxynucleotides. Expand
Elaborated Action of the Human Primosome
The human primosome is a 340-kilodalton complex of primase (DNA-dependent RNA polymerase) and DNA polymerase α, which initiates genome replication by synthesizing chimeric RNA-DNA primers for DNAExpand
Structure of a bifunctional DNA primase-polymerase
It is proposed that archaeal and eukaryotic primases and the prim-pol domain have a common evolutionary ancestor, a bifunctional replicase for small DNA genomes. Expand
Insight into the Human DNA Primase Interaction with Template-Primer*
It is shown that the C-terminal domain of the large subunit (p58C) plays a major role in template-primer binding and also defines the elements of the DNA template and the RNA primer that interact with p58C. Expand
The DNA Polymerase ʱ-Primase Complex: Multiple Functions and Interactions
The major role of the DNA polymerase _-primase complex (pol-prim) is in the initiation of DNA replication at chromosomal origins and in the discontinuous synthesis of Okazaki fragments on the lagging strand of the replication fork. Expand
Structure of the heterodimeric core primase
A crystallographic and biochemical analysis of the core primase from the archaeon Sulfolobus solfataricus is reported, providing the first three-dimensional description of the large subunit and its interaction with the small subunit. Expand
The DNA primase of Sulfolobus solfataricus is activated by substrates containing a thymine-rich bubble and has a 3'-terminal nucleotidyl-transferase activity.
Interestingly, the Sso DNA primase complex is endowed with a terminal nucleotidyl-transferase activity, being able to incorporate nucleotides at the 3' end of synthetic oligonucleotides in a non-templated manner. Expand
The C-terminal Domain of the DNA Polymerase Catalytic Subunit Regulates the Primase and Polymerase Activities of the Human DNA Polymerase α-Primase Complex*
It is found that polα activity strongly depends on the sequence of the template and that homopyrimidine runs create a strong barrier for DNA synthesis by polα, which regulates the proper primase and polymerase function. Expand
A novel type of replicative enzyme harbouring ATPase, primase and DNA polymerase activity
A new type of replication protein that constitutes the first member of the DNA polymerase family E. ORF904, encoded by the plasmid pRN1 from the thermoacidophile archaeon Sulfolobus islandicus, is a highly compact multifunctional enzyme with ATPase, primase andDNA polymerase activity. Expand
Crystal structure of the C-terminal domain of human DNA primase large subunit
A mechanism of RNA primer length counting and dissociation of the primer-template from primase by a switch in conformation of the ssDNA-binding region of p58 is proposed. Expand