Optimization of Recombinant Human Poly(ADP-ribose) Polymerase 3 Production

PARP3 (Poly(ADP-ribose) polymerase 3), like other PARP family members (PARP1 and PARP2), is an important factor in DNA repair. The specific functions and molecular mechanisms of action of this protein remain insufficiently studied. The development of a reliable protocol for obtaining high-purity and yield PARP3 is essential for comprehensive protein analysis, enzymatic activity, including studies of its binding to DNA, interactions with other protein factors, and structural investigations. In this study, we present a modified protocol for the expression of human PARP3 from Escherichia coli cells and its subsequent purification, which significantly increases protein yield compared to previously published methods.

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Publication Details

Journal
Moscow University Biological Sciences Bulletin
Published
2025-12-01
DOI
https://doi.org/10.3103/s009639252560098x
Citations
1
Primary Topic
PARP inhibition in cancer therapy
Type
article
Field-Weighted Citation Impact
1.05
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article

Optimization of Recombinant Human Poly(ADP-ribose) Polymerase 3 Production

E. A. Volkova, N. V. Maluchenko, V. M. Studitsky, A. N. Korovina
1 citations
Moscow University Biological Sciences Bulletin
PARP inhibition in cancer therapy
1.05
article

Optimization of Recombinant Human Poly(ADP-ribose) Polymerase 3 Production

E. A. Volkova, N. V. Maluchenko, V. M. Studitsky, A. N. Korovina
article en
1 citations

Abstract

PARP3 (Poly(ADP-ribose) polymerase 3), like other PARP family members (PARP1 and PARP2), is an important factor in DNA repair. The specific functions and molecular mechanisms of action of this protein remain insufficiently studied. The development of a reliable protocol for obtaining high-purity and yield PARP3 is essential for comprehensive protein analysis, enzymatic activity, including studies of its binding to DNA, interactions with other protein factors, and structural investigations. In this study, we present a modified protocol for the expression of human PARP3 from Escherichia coli cells and its subsequent purification, which significantly increases protein yield compared to previously published methods.

Moscow University Biological Sciences BulletinVol. 80(S1)
Fox Chase Cancer Center (US), Lomonosov Moscow State University (RU)
Openalex Percentile: Top 15%
PARP inhibition in cancer therapy
1.05
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