ArticleACS chemical biology2013
Site-specific noncovalent interaction of the biopolymer poly(ADP-ribose) with the Werner syndrome protein regulates protein functions.
Article in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 43 citations in OpenAlex.
- RECQL4 requires PARP1 for recruitment to DNA damage, and PARG dePARylation facilitates its associated role in end joining.Experimental & molecular medicine · 2025Article
- Single-molecule imaging of genome maintenance proteins encountering specific DNA sequences and structures.DNA repair · 2023Review
- Influence of chain length and branching on poly(ADP-ribose)-protein interactions.Nucleic acids research · 2023Article
- Functions of ADP-ribose transferases in the maintenance of telomere integrity.Cellular and molecular life sciences : CMLS · 2022Review
- ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological Perspectives.Biomolecules · 2022Review
- Why structure and chain length matter: on the biological significance underlying the structural heterogeneity of poly(ADP-ribose).Nucleic acids research · 2021Article
- ADP-ribosylation of histone variant H2AX promotes base excision repair.The EMBO journal · 2021Article
- Functional Roles of Poly(ADP-Ribose) in Stress Granule Formation and Dynamics.Frontiers in cell and developmental biology · 2021Review
- PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response.Nucleic acids research · 2020Article
- Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation.Trends in cell biology · 2020Review
- PARP1 regulates DNA damage-induced nucleolar-nucleoplasmic shuttling of WRN and XRCC1 in a toxicant and protein-specific manner.Scientific reports · 2019Article
- ELTA: Enzymatic Labeling of Terminal ADP-Ribose.Molecular cell · 2019Article
- Multiple Roles for Mono- and Poly(ADP-Ribose) in Regulating Stress Responses.Trends in genetics : TIG · 2019Review
- The C-terminal domain of p53 orchestrates the interplay between non-covalent and covalent poly(ADP-ribosyl)ation of p53 by PARP1.Nucleic acids research · 2018Article
- PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions.Scientific reports · 2017Article
- Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NADBeilstein journal of organic chemistry · 2017Article
- Different non-synonymous polymorphisms modulate the interaction of the WRN protein to its protein partners and its enzymatic activities.Oncotarget · 2016Article
- Analyzing structure-function relationships of artificial and cancer-associated PARP1 variants by reconstituting TALEN-generated HeLa PARP1 knock-out cells.Nucleic acids research · 2016Article
- Readers of poly(ADP-ribose): designed to be fit for purpose.Nucleic acids research · 2016Review
- Differential and Concordant Roles for Poly(ADP-Ribose) Polymerase 1 and Poly(ADP-Ribose) in Regulating WRN and RECQL5 Activities.Molecular and cellular biology · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Werner syndrome is a premature aging disorder that is caused by defects in the Werner protein (WRN). WRN is a member of the RecQ helicase family and possesses helicase and exonuclease activities. It is involved in various aspects of DNA metabolism such as DNA repair, telomere maintenance, and replication. Poly(ADP-ribose) polymerase 1 (PARP1) is also involved in these processes by catalyzing the formation of the nucleic-acid-like biopolymer poly(ADP-ribose) (PAR). It was previously shown that WRN interacts with PARP1 and that WRN activity is inhibited by PARP1. Using several bioanalytical approaches, here we demonstrate that the enzymatic product of PARP1, i.e., PAR, directly interacts with WRN physically and functionally. First, WRN binds HPLC-size-fractionated short and long PAR in a noncovalent manner. Second, we identified and characterized a PAR-binding motif (PBM) within the WRN sequence and showed that several basic and hydrophobic amino acids are of critical importance for mediating the PAR binding. Third, PAR-binding inhibits the DNA-binding, the helicase and the exonuclease activities of WRN in a concentration-dependent manner. On the basis of our results we propose that the transient nature of PAR produced by living cells would provide a versatile and swiftly reacting control system for WRN's function. More generally, our work underscores the important role of noncovalent PAR-protein interactions as a regulatory mechanism of protein function.
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