Y-box-binding protein 1 as a non-canonical factor of base excision repair
Copyright © 2016 Elsevier B.V. All rights reserved..
Base excision repair (BER) is a flagship DNA repair system responsible for maintaining genome integrity. Apart from basal enzymes, this system involves several accessory factors essential for coordination and regulation of DNA processing during substrate channeling. Y-box-binding protein 1 (YB-1), a multifunctional factor that can interact with DNA, RNA, poly(ADP-ribose) and plenty of proteins including DNA repair enzymes, is increasingly considered as a non-canonical protein of BER. Here we provide quantitative characterization of YB-1 physical interactions with key BER factors such as PARP1, PARP2, APE1, NEIL1 and pol β and comparison of the full-length YB-1 and its C-terminally truncated nuclear form in regard to their binding affinities for BER proteins. Data on functional interactions reveal strong stimulation of PARP1 autopoly(ADP-ribosyl)ation and inhibition of poly(ADP-ribose) degradation by PARG in the presence of YB-1. Moreover, YB-1 is shown to stimulate AP lyase activity of NEIL1 and to inhibit dRP lyase activity of pol β on model DNA duplex structure. We also demonstrate for the first time YB-1 poly(ADP-ribosyl)ation in the presence of RNA.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2016 |
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| Erschienen: |
2016 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:1864 |
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| Enthalten in: |
Biochimica et biophysica acta - 1864(2016), 12 vom: 15. Dez., Seite 1631-1640 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Alemasova, Elizaveta E [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 28.01.2019 Date Revised 09.12.2020 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.bbapap.2016.08.012 |
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| Förderinstitution / Projekttitel: |
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| 245 | 1 | 0 | |a Y-box-binding protein 1 as a non-canonical factor of base excision repair |
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| 500 | |a Date Revised 09.12.2020 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2016 Elsevier B.V. All rights reserved. | ||
| 520 | |a Base excision repair (BER) is a flagship DNA repair system responsible for maintaining genome integrity. Apart from basal enzymes, this system involves several accessory factors essential for coordination and regulation of DNA processing during substrate channeling. Y-box-binding protein 1 (YB-1), a multifunctional factor that can interact with DNA, RNA, poly(ADP-ribose) and plenty of proteins including DNA repair enzymes, is increasingly considered as a non-canonical protein of BER. Here we provide quantitative characterization of YB-1 physical interactions with key BER factors such as PARP1, PARP2, APE1, NEIL1 and pol β and comparison of the full-length YB-1 and its C-terminally truncated nuclear form in regard to their binding affinities for BER proteins. Data on functional interactions reveal strong stimulation of PARP1 autopoly(ADP-ribosyl)ation and inhibition of poly(ADP-ribose) degradation by PARG in the presence of YB-1. Moreover, YB-1 is shown to stimulate AP lyase activity of NEIL1 and to inhibit dRP lyase activity of pol β on model DNA duplex structure. We also demonstrate for the first time YB-1 poly(ADP-ribosyl)ation in the presence of RNA | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Base excision repair (BER) regulation | |
| 650 | 4 | |a PARP1(2) | |
| 650 | 4 | |a Poly(ADP-ribose) (PAR) | |
| 650 | 4 | |a RNA | |
| 650 | 4 | |a Y-box binding protein 1 (YB-1) | |
| 650 | 7 | |a Peptide Fragments |2 NLM | |
| 650 | 7 | |a Recombinant Proteins |2 NLM | |
| 650 | 7 | |a Y-Box-Binding Protein 1 |2 NLM | |
| 650 | 7 | |a YBX1 protein, human |2 NLM | |
| 650 | 7 | |a PARP1 protein, human |2 NLM | |
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| 650 | 7 | |a Poly(ADP-ribose) Polymerases |2 NLM | |
| 650 | 7 | |a EC 2.4.2.30 |2 NLM | |
| 650 | 7 | |a Parp2 protein, mouse |2 NLM | |
| 650 | 7 | |a EC 2.4.2.30. |2 NLM | |
| 650 | 7 | |a DNA Polymerase beta |2 NLM | |
| 650 | 7 | |a EC 2.7.7.7 |2 NLM | |
| 650 | 7 | |a POLB protein, human |2 NLM | |
| 650 | 7 | |a EC 2.7.7.7 |2 NLM | |
| 650 | 7 | |a DNA Glycosylases |2 NLM | |
| 650 | 7 | |a EC 3.2.2.- |2 NLM | |
| 650 | 7 | |a NEIL1 protein, human |2 NLM | |
| 650 | 7 | |a EC 3.2.2.- |2 NLM | |
| 650 | 7 | |a APEX1 protein, human |2 NLM | |
| 650 | 7 | |a EC 4.2.99.18 |2 NLM | |
| 650 | 7 | |a DNA-(Apurinic or Apyrimidinic Site) Lyase |2 NLM | |
| 650 | 7 | |a EC 4.2.99.18 |2 NLM | |
| 700 | 1 | |a Moor, Nina A |e verfasserin |4 aut | |
| 700 | 1 | |a Naumenko, Konstantin N |e verfasserin |4 aut | |
| 700 | 1 | |a Kutuzov, Mikhail M |e verfasserin |4 aut | |
| 700 | 1 | |a Sukhanova, Maria V |e verfasserin |4 aut | |
| 700 | 1 | |a Pestryakov, Pavel E |e verfasserin |4 aut | |
| 700 | 1 | |a Lavrik, Olga I |e verfasserin |4 aut | |
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