Purification of DNA Repair Enzymes

E. coli Fpg protein [40 (link)], human OGG1 protein [104 (link)], human POLκ (catalytic core, residues 1–560) [105 (link)], POLβ [106 (link)], POLλ [107 (link)], PrimPol [72 (link)], human DNA polymerase η (hPOLη) [72 (link)] and yeast DNA polymerase η (yPOLη) [108 (link)] were essentially overexpressed and purified as described. E. coli uracil–DNA glycosylase (Ung) was purchased from SibEnzyme (Novosibirsk, Russia) and trypsin was purchased from Samson-Med (St. Petersburg, Russia). Oligonucleotides (Table 2) were synthesized in-house from commercially available phosphoramidites (Glen Research, Sterling, VA, USA).

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Yudkina A.V., Barmatov A.E., Bulgakov N.A., Boldinova E.O., Shilkin E.S., Makarova A.V, & Zharkov D.O. (2023). Bypass of Abasic Site–Peptide Cross-Links by Human Repair and Translesion DNA Polymerases. International Journal of Molecular Sciences, 24(13), 10877.

Publication 2023

phosphoramidites

Catalytic core Dna polymerase η E coli E coli fpg protein Human Human ogg1 protein Oligonucleotides Phosphoramidites Trypsin Uracil dna glycosylase Yeast

Corresponding Organization : Novosibirsk State University

Other organizations : Kurchatov Institute, Institute of Molecular Genetics

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Variable analysis

independent variables

E. coli Fpg protein
Human OGG1 protein
Human POLκ (catalytic core, residues 1–560)
POLβ
POLλ
PrimPol
Human DNA polymerase η (hPOLη)
Yeast DNA polymerase η (yPOLη)
E. coli uracil–DNA glycosylase (Ung)
Trypsin

dependent variables

Not explicitly mentioned

control variables

Oligonucleotides (Table 2) were synthesized in-house from commercially available phosphoramidites (Glen Research, Sterling, VA, USA).

controls

Positive control: Not specified
Negative control: Not specified

Annotations

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