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Literature summary for 4.1.99.3 extracted from

  • Sauguet, L.; Klinge, S.; Perera, R.L.; Maman, J.D.; Pellegrini, L.
    Shared active site architecture between the large subunit of eukaryotic primase and DNA photolyase (2010), PLoS ONE, 5, e10083.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
PriL-CTD construct where the 381-RNG-383 sequence is excised, expressed in Escherichia coli strain BL21(DE3) Rosetta2. Full-length and C-terminally truncated primase Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Fe conserved Fe-S domain at the C-terminus of PriL Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
-

Purification (Commentary)

Purification (Comment) Organism
by Co-NTA and heparin chromatography followed by TEV protease cleavage of the tag and gel filtration. Full-length and C-terminally truncated primase Saccharomyces cerevisiae

Storage Stability

Storage Stability Organism
-80°C, 20 mM Hepes buffer, pH 6.8, 200 mM KCl, 3 mM TCEP Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclobutadipyrimidine in DNA the larger N-terminal domain of primase carboxy-terminal domain (PriL-CTD) assists the smaller catalytic subunit PriS in the simultaneous binding of the two initial ribonucleotides and in promoting their Watson-Crick base pairing at the initiation site on the template DNA Saccharomyces cerevisiae ?
-
?

Synonyms

Synonyms Comment Organism
DNA photolyase
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Saccharomyces cerevisiae
primase
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Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function structural similarity between the larger N-terminal domain of primase (PriL) with the active site region of DNA photolyase Saccharomyces cerevisiae