Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1
Y-box-binding protein 1 (YB-1) is a multifunctional positively charged protein that interacts with DNA or RNA and poly(ADP-ribose) (PAR). YB-1 is poly(ADP-ribosyl)ated and stimulates poly(ADP-ribose) polymerase 1 (PARP1) activity. Here, we studied the mechanism of YB-1-dependent PAR synthesis by PAR...
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doaj-2ccb3ea8872a487e8a10a3dbcc006a742020-11-25T03:28:48ZengMDPI AGBiomolecules2218-273X2020-09-01101325132510.3390/biom10091325Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1Konstantin N. Naumenko0Mariya V. Sukhanova1Loic Hamon2Tatyana A. Kurgina3Elizaveta E. Alemasova4Mikhail M. Kutuzov5David Pastré6Olga I. Lavrik7Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk 630090, RussiaInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk 630090, RussiaLaboratoire Structure-Activité des Biomolécules Normales et Pathologiques, University of Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, FranceInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk 630090, RussiaInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk 630090, RussiaInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk 630090, RussiaLaboratoire Structure-Activité des Biomolécules Normales et Pathologiques, University of Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, FranceInstitute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk 630090, RussiaY-box-binding protein 1 (YB-1) is a multifunctional positively charged protein that interacts with DNA or RNA and poly(ADP-ribose) (PAR). YB-1 is poly(ADP-ribosyl)ated and stimulates poly(ADP-ribose) polymerase 1 (PARP1) activity. Here, we studied the mechanism of YB-1-dependent PAR synthesis by PARP1 in vitro using biochemical and atomic force microscopy assays. PAR synthesis activity of PARP1 is known to be facilitated by co-factors such as Mg<sup>2+</sup>. However, in contrast to an Mg<sup>2+</sup>-dependent reaction, the activation of PARP1 by YB-1 is accompanied by overall up-regulation of protein PARylation and shortening of the PAR polymer. Therefore, YB-1 and cation co-factors stimulated PAR synthesis in divergent ways. PARP1 autoPARylation in the presence of YB-1 as well as trans-PARylation of YB-1 are greatly affected by the type of damaged DNA, suggesting that PARP1 activation depends on the formation of a PARP1–YB-1–DNA ternary complex. An unstructured C-terminal part of YB-1 involved in an interaction with PAR behaves similarly to full-length YB-1, indicating that both DNA and PAR binding are involved in the stimulation of PARP1 activity by YB-1. Thus, YB-1 is likely linked to the regulation of PARylation events in cells via an interaction with PAR and damaged DNA.https://www.mdpi.com/2218-273X/10/9/1325Y-box-binding protein 1poly(ADP-ribose) polymerase 1protein poly(ADP-ribosyl)ation |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Konstantin N. Naumenko Mariya V. Sukhanova Loic Hamon Tatyana A. Kurgina Elizaveta E. Alemasova Mikhail M. Kutuzov David Pastré Olga I. Lavrik |
spellingShingle |
Konstantin N. Naumenko Mariya V. Sukhanova Loic Hamon Tatyana A. Kurgina Elizaveta E. Alemasova Mikhail M. Kutuzov David Pastré Olga I. Lavrik Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1 Biomolecules Y-box-binding protein 1 poly(ADP-ribose) polymerase 1 protein poly(ADP-ribosyl)ation |
author_facet |
Konstantin N. Naumenko Mariya V. Sukhanova Loic Hamon Tatyana A. Kurgina Elizaveta E. Alemasova Mikhail M. Kutuzov David Pastré Olga I. Lavrik |
author_sort |
Konstantin N. Naumenko |
title |
Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1 |
title_short |
Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1 |
title_full |
Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1 |
title_fullStr |
Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1 |
title_full_unstemmed |
Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1 |
title_sort |
regulation of poly(adp-ribose) polymerase 1 activity by y-box-binding protein 1 |
publisher |
MDPI AG |
series |
Biomolecules |
issn |
2218-273X |
publishDate |
2020-09-01 |
description |
Y-box-binding protein 1 (YB-1) is a multifunctional positively charged protein that interacts with DNA or RNA and poly(ADP-ribose) (PAR). YB-1 is poly(ADP-ribosyl)ated and stimulates poly(ADP-ribose) polymerase 1 (PARP1) activity. Here, we studied the mechanism of YB-1-dependent PAR synthesis by PARP1 in vitro using biochemical and atomic force microscopy assays. PAR synthesis activity of PARP1 is known to be facilitated by co-factors such as Mg<sup>2+</sup>. However, in contrast to an Mg<sup>2+</sup>-dependent reaction, the activation of PARP1 by YB-1 is accompanied by overall up-regulation of protein PARylation and shortening of the PAR polymer. Therefore, YB-1 and cation co-factors stimulated PAR synthesis in divergent ways. PARP1 autoPARylation in the presence of YB-1 as well as trans-PARylation of YB-1 are greatly affected by the type of damaged DNA, suggesting that PARP1 activation depends on the formation of a PARP1–YB-1–DNA ternary complex. An unstructured C-terminal part of YB-1 involved in an interaction with PAR behaves similarly to full-length YB-1, indicating that both DNA and PAR binding are involved in the stimulation of PARP1 activity by YB-1. Thus, YB-1 is likely linked to the regulation of PARylation events in cells via an interaction with PAR and damaged DNA. |
topic |
Y-box-binding protein 1 poly(ADP-ribose) polymerase 1 protein poly(ADP-ribosyl)ation |
url |
https://www.mdpi.com/2218-273X/10/9/1325 |
work_keys_str_mv |
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