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碱基切除修复中的蛋白质-蛋白质相互作用

Protein-Protein Interactions in Base Excision Repair.

作者信息

Rathnaiah Govardhan, Sweasy Joann B

机构信息

Fred and Pamela Buffett Cancer Center and Eppley Institute for Cancer Research, Omaha, NE 68198, USA.

出版信息

Biomolecules. 2025 Jun 18;15(6):890. doi: 10.3390/biom15060890.


DOI:10.3390/biom15060890
PMID:40563529
Abstract

The Base Excision Repair (BER) pathway involves a highly coordinated series of protein-protein interactions that facilitate the recognition, excision, and repair of damaged bases. Key enzymes such as DNA glycosylases, apurinic/apyrimidinic endonuclease 1 (APE1), polynucleotide kinase-phosphatase (PNKP), DNA polymerase b (Pol β), ligase IIIα (LigIIIα), poly (ADP-ribose) polymerases PARP1 and PARP2, and X-ray repair cross-complementing protein 1 (XRCC1) catalyze BER in a tightly regulated molecular network. These interactions ensure the seamless handoff of DNA intermediates between the core enzymes of the BER pathway. Understanding the details of protein-protein interactions in BER provides valuable insights into the molecular underpinnings of DNA repair processes. In this review, we focus on protein-protein interactions between the components of the single-nucleotide BER (SN-BER) pathway and other proteins that interact with BER components and regulate the coordination of the pathway. We also briefly discuss the interactions of other proteins that interact with the components of SN-BER based on functional evidence.

摘要

碱基切除修复(BER)途径涉及一系列高度协调的蛋白质-蛋白质相互作用,这些相互作用促进了对受损碱基的识别、切除和修复。关键酶如DNA糖基化酶、脱嘌呤/脱嘧啶内切核酸酶1(APE1)、多核苷酸激酶-磷酸酶(PNKP)、DNA聚合酶β(Pol β)、连接酶IIIα(LigIIIα)、聚(ADP-核糖)聚合酶PARP1和PARP2以及X射线修复交叉互补蛋白1(XRCC1)在一个严格调控的分子网络中催化BER。这些相互作用确保了BER途径核心酶之间DNA中间体的无缝交接。了解BER中蛋白质-蛋白质相互作用的细节为深入了解DNA修复过程的分子基础提供了有价值的见解。在本综述中,我们重点关注单核苷酸BER(SN-BER)途径各组分之间的蛋白质-蛋白质相互作用,以及与BER组分相互作用并调节该途径协调性的其他蛋白质。我们还根据功能证据简要讨论了与SN-BER组分相互作用的其他蛋白质的相互作用。

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[1]
Protein-Protein Interactions in Base Excision Repair.

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[2]
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[3]
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[4]
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[5]
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[6]
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[7]
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[8]
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本文引用的文献

[1]
Molecular basis and functional consequences of the interaction between the base excision repair DNA glycosylase NEIL1 and RPA.

J Biol Chem. 2024-9

[2]
Apurinic/apyrimidinic endonuclease 1 has major impact in prevention of suicidal covalent DNA-protein crosslink with apurinic/apyrimidinic site in cellular extracts.

IUBMB Life. 2024-11

[3]
Human CST Stimulates Base Excision Repair to Prevent the Accumulation of Oxidative DNA Damage.

J Mol Biol. 2024-8-15

[4]
The dynamics and regulation of PARP1 and PARP2 in response to DNA damage and during replication.

DNA Repair (Amst). 2024-8

[5]
Impact of DNA ligase 1 and IIIα interactions with APE1 and polβ on the efficiency of base excision repair pathway at the downstream steps.

J Biol Chem. 2024-6

[6]
Human NTHL1 expression and subcellular distribution determines cisplatin sensitivity in human lung epithelial and non-small cell lung cancer cells.

NAR Cancer. 2024-2-21

[7]
Covalent PARylation of DNA base excision repair proteins regulates DNA demethylation.

Nat Commun. 2024-1-2

[8]
Coordination between human DNA polymerase β and apurinic/apyrimidinic endonuclease 1 in the course of DNA repair.

Biochimie. 2024-1

[9]
The Role of Poly(ADP-ribose) Polymerase 1 in Nuclear and Mitochondrial Base Excision Repair.

Biomolecules. 2023-7-31

[10]
The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates.

Int J Mol Sci. 2023-5-31

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