Poly(ADP‐ribose)‐mediated interplay of XPA and PARP 1 leads to reciprocal regulation of protein function
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Poly(ADP‐ribose) (PAR) is a complex and reversible post‐translational modification that controls protein function and localization through covalent modification of, or noncovalent binding to target proteins. Previously, we and others characterized the noncovalent, high‐affinity binding of the key nucleotide excision repair (NER) protein XPA to PAR. In the present study, we address the functional relevance of this interaction. First, we confirm that pharmacological inhibition of cellular poly(ADP‐ribosyl)ation (PAR ylation) impairs NER efficacy. Second, we demonstrate that the XPA–PAR interaction is mediated by specific basic amino acids within a highly conserved PAR‐binding motif, which overlaps the DNA damage‐binding protein 2 (DDB 2) and transcription factor II H (TFIIH) interaction domains of XPA. Third, biochemical studies reveal a mutual regulation of PARP 1 and XPA functions showing that, on the one hand, the XPA–PAR interaction lowers the DNA binding affinity of XPA, whereas, on the other hand, XPA itself strongly stimulates PARP 1 enzymatic activity. Fourth, microirradiation experiments in U2 OS cells demonstrate that PARP inhibition alters the recruitment properties of XPA‐green fluorescent protein to sites of laser‐induced DNA damage. In conclusion, our results reveal that XPA and PARP 1 regulate each other in a reciprocal and PAR‐dependent manner, potentially acting as a fine‐tuning mechanism for the spatio‐temporal regulation of the two factors during NER.
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XPA and PARP1 appear to have regulatory interactions that would be disrupted in XPA−/− cells.
“In addition, XPA and PARP1 appear to have regulatory interactions which would be upset in the XPA−/− cells99.”
From Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation (2017) · cites this paper as [99]
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- Authors
- Fischer, J. M. F., Popp, O., Gebhard, D., Veith, S., Fischbach, A., Beneke, S., Leitenstorfer, A., Bergemann, J., Scheffner, M., Ferrando‐May, E., Mangerich, A., & Bürkle, A.
- Affiliations
- University of Konstanz (DE)
- Albstadt-Sigmaringen University (DE)
- Corresponding author
- Mangerich, Aswin
- ORCID
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2014-07-21
- Volume
- 281
- Issue
- 16
- Pages
- 3625-3641
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- PMC
- PMC4160017
- OpenAlex
- W2077377040
- Cited by
- 72
- References
- 53
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 3 · 2023: 5 · 2022: 5 · 2021: 7 · 2020: 7 · 2019: 5 · 2018: 4 · 2017: 8 · 2016: 11 · 2015: 10 · 2014: 2
- FWCI
- 4.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- FEBS Journal (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- KOPS (University of Konstanz) (submittedVersion, cc-by)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Health Sciences › Medicine › Pathology and Forensic Medicine › Genetic factors in colorectal cancer
- Keywords
- poly(ADP-ribose), poly(ADP-ribosyl)ation, XPA, PARP1, nucleotide excision repair, DDB2, TFIIH, DNA damage response, PARP inhibition, DNA binding affinity, protein-protein interaction, U2OS cells
- MeSH terms
- Poly (ADP-Ribose) Polymerase-1, Amino Acid Sequence, DNA Repair, HeLa Cells, Humans, Kinetics, Molecular Sequence Data, Poly Adenosine Diphosphate Ribose, Poly(ADP-ribose) Polymerases, Protein Binding, Protein Processing, Post-Translational, Consensus Sequence, Xeroderma Pigmentosum Group A Protein, Sf9 Cells
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