The C-Terminal Domain of Y-Box Binding Protein 1 Exhibits Structure-Specific Binding to Poly(ADP-Ribose), Which Regulates PARP1 Activity

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2022
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Naumenko, Konstantin N.
Sukhanova, Mariya V.
Hamon, Loic
Kurgina, Tatyana A.
Anarbaev, Rashid O.
Pastré, David
Lavrik, Olga I.
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Frontiers in Cell and Developmental Biology. Frontiers Media. 2022, 10, 831741. eISSN 2296-634X. Available under: doi: 10.3389/fcell.2022.831741
Zusammenfassung

Y-box-binding protein 1 (YB-1) is a multifunctional protein involved in the regulation of gene expression. Recent studies showed that in addition to its role in the RNA and DNA metabolism, YB-1 is involved in the regulation of PARP1 activity, which catalyzes poly(ADP-ribose) [PAR] synthesis under genotoxic stress through auto-poly(ADP-ribosyl)ation or protein trans-poly(ADP-ribosyl)ation. Nonetheless, the exact mechanism by which YB-1 regulates PAR synthesis remains to be determined. YB-1 contains a disordered Ala/Pro-rich N-terminal domain, a cold shock domain, and an intrinsically disordered C-terminal domain (CTD) carrying four clusters of positively charged amino acid residues. Here, we examined the functional role of the disordered CTD of YB-1 in PAR binding and in the regulation of PARP1-driven PAR synthesis in vitro. We demonstrated that the rate of PARP1-dependent synthesis of PAR is higher in the presence of YB-1 and is tightly controlled by the interaction between YB-1 CTD and PAR. Moreover, YB-1 acts as an effective cofactor in the PAR synthesis catalyzed by the PARP1 point mutants that generate various PAR polymeric structures, namely, short hypo- or hyperbranched polymers. We showed that either a decrease in chain length or an increase in branching frequency of PAR affect its binding affinity for YB-1 and YB-1–mediated stimulation of PARP1 enzymatic activity. These results provide important insight into the mechanism underlying the regulation of PARP1 activity by PAR-binding proteins containing disordered regions with clusters of positively charged amino acid residues, suggesting that YB-1 CTD-like domains may be considered PAR “readers” just as other known PAR-binding modules.

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570 Biowissenschaften, Biologie
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Y-box binding protein 1, PARP1, trans-poly(ADP-ribosyl) ation, poly(ADP-ribose), disordered C-terminal domain
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ISO 690NAUMENKO, Konstantin N., Mariya V. SUKHANOVA, Loic HAMON, Tatyana A. KURGINA, Rashid O. ANARBAEV, Aswin MANGERICH, David PASTRÉ, Olga I. LAVRIK, 2022. The C-Terminal Domain of Y-Box Binding Protein 1 Exhibits Structure-Specific Binding to Poly(ADP-Ribose), Which Regulates PARP1 Activity. In: Frontiers in Cell and Developmental Biology. Frontiers Media. 2022, 10, 831741. eISSN 2296-634X. Available under: doi: 10.3389/fcell.2022.831741
BibTex
@article{Naumenko2022-06-21CTerm-57847,
  year={2022},
  doi={10.3389/fcell.2022.831741},
  title={The C-Terminal Domain of Y-Box Binding Protein 1 Exhibits Structure-Specific Binding to Poly(ADP-Ribose), Which Regulates PARP1 Activity},
  volume={10},
  journal={Frontiers in Cell and Developmental Biology},
  author={Naumenko, Konstantin N. and Sukhanova, Mariya V. and Hamon, Loic and Kurgina, Tatyana A. and Anarbaev, Rashid O. and Mangerich, Aswin and Pastré, David and Lavrik, Olga I.},
  note={Article Number: 831741}
}
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