دورية أكاديمية

PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling

التفاصيل البيبلوغرافية
العنوان: PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling
المؤلفون: Lotte van Beek, Éilís McClay, Saleha Patel, Marianne Schimpl, Laura Spagnolo, Taiana Maia de Oliveira
المصدر: International Journal of Molecular Sciences, Vol 22, Iss 10, p 5112 (2021)
بيانات النشر: MDPI AG, 2021.
سنة النشر: 2021
المجموعة: LCC:Biology (General)
LCC:Chemistry
مصطلحات موضوعية: Poly (ADP-ribose) polymerases 1-3, DNA damage response, PARP-DNA binding, ADP-ribosylation, nucleosome remodelling, histone PARylation factor 1, Biology (General), QH301-705.5, Chemistry, QD1-999
الوصف: Poly (ADP-ribose) polymerases (PARP) 1-3 are well-known multi-domain enzymes, catalysing the covalent modification of proteins, DNA, and themselves. They attach mono- or poly-ADP-ribose to targets using NAD+ as a substrate. Poly-ADP-ribosylation (PARylation) is central to the important functions of PARP enzymes in the DNA damage response and nucleosome remodelling. Activation of PARP happens through DNA binding via zinc fingers and/or the WGR domain. Modulation of their activity using PARP inhibitors occupying the NAD+ binding site has proven successful in cancer therapies. For decades, studies set out to elucidate their full-length molecular structure and activation mechanism. In the last five years, significant advances have progressed the structural and functional understanding of PARP1-3, such as understanding allosteric activation via inter-domain contacts, how PARP senses damaged DNA in the crowded nucleus, and the complementary role of histone PARylation factor 1 in modulating the active site of PARP. Here, we review these advances together with the versatility of PARP domains involved in DNA binding, the targets and shape of PARylation and the role of PARPs in nucleosome remodelling.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1422-0067
1661-6596
العلاقة: https://www.mdpi.com/1422-0067/22/10/5112Test; https://doaj.org/toc/1661-6596Test; https://doaj.org/toc/1422-0067Test
DOI: 10.3390/ijms22105112
الوصول الحر: https://doaj.org/article/330724b4ce614e97af4b4e2129d27fe4Test
رقم الانضمام: edsdoj.330724b4ce614e97af4b4e2129d27fe4
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:14220067
16616596
DOI:10.3390/ijms22105112