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 | Comment | Organism | Structure |
---|---|---|---|
Fe | conserved Fe-S domain at the C-terminus of PriL | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
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 | Organism |
---|---|
-80°C, 20 mM Hepes buffer, pH 6.8, 200 mM KCl, 3 mM TCEP | Saccharomyces cerevisiae |
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 | Comment | Organism |
---|---|---|
DNA photolyase | - |
Saccharomyces cerevisiae |
primase | - |
Saccharomyces cerevisiae |
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 |