DNA Repair最新文献_第10页

MutS recognition of mismatches within primed DNA replication intermediates MutS对引物DNA复制中间体错配的识别

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-11-01 DOI: 10.1016/j.dnarep.2022.103392

Milagros Inés Ibáñez Busseti , Lucía Malvina Margara , Sofía Daiana Castell , Marisa Mariel Fernández , Emilio Luis Malchiodi , Guillermo Gabriel Montich , Virginia Miguel , Carlos Enrique Argaraña , Mariela Roxana Monti

{"title":"MutS recognition of mismatches within primed DNA replication intermediates","authors":"Milagros Inés Ibáñez Busseti , Lucía Malvina Margara , Sofía Daiana Castell , Marisa Mariel Fernández , Emilio Luis Malchiodi , Guillermo Gabriel Montich , Virginia Miguel , Carlos Enrique Argaraña , Mariela Roxana Monti","doi":"10.1016/j.dnarep.2022.103392","DOIUrl":"https://doi.org/10.1016/j.dnarep.2022.103392","url":null,"abstract":"<div>MutS initiates mismatch repair by recognizing mismatches in newly replicated DNA. Specific interactions between MutS and mismatches within double-stranded DNA promote ADP-ATP exchange and a conformational change into a sliding clamp. Here, we demonstrated that MutS from Pseudomonas aeruginosa associates with primed DNA replication intermediates. The predicted structure of this MutS-DNA complex revealed a new DNA binding site, in which Asn 279 and Arg 272 appeared to directly interact with the 3′-OH terminus of primed DNA. Mutation of these residues resulted in a noticeable defect in the interaction of MutS with primed DNA substrates. Remarkably, MutS interaction with a mismatch within primed DNA induced a compaction of the protein structure and impaired the formation of an ATP-bound sliding clamp. Our findings reveal a novel DNA binding mode, conformational change and intramolecular signaling for MutS recognition of mismatches within primed DNA structures.</div>","PeriodicalId":300,"journal":{"name":"DNA Repair","volume":"119 ","pages":"Article 103392"},"PeriodicalIF":3.8,"publicationDate":"2022-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"3081576","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

From fluorescent foci to sequence: Illuminating DNA double strand break repair by high-throughput sequencing technologies 从荧光焦点到序列:用高通量测序技术照亮DNA双链断裂修复

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-10-01 DOI: 10.1016/j.dnarep.2022.103388

Xabier Vergara , Ruben Schep , René H. Medema , Bas van Steensel

引用次数: 1

A redox-sensitive iron-sulfur cluster in murine FAM72A controls its ability to degrade the nuclear form of uracil-DNA glycosylase 小鼠FAM72A中的氧化还原敏感铁硫簇控制其降解尿嘧啶- dna糖基酶核形式的能力

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-10-01 DOI: 10.1016/j.dnarep.2022.103381

Jessica A. Stewart , Ashok S. Bhagwat

{"title":"A redox-sensitive iron-sulfur cluster in murine FAM72A controls its ability to degrade the nuclear form of uracil-DNA glycosylase","authors":"Jessica A. Stewart , Ashok S. Bhagwat","doi":"10.1016/j.dnarep.2022.103381","DOIUrl":"https://doi.org/10.1016/j.dnarep.2022.103381","url":null,"abstract":"<div>Murine FAM72A, mFAM72A, binds the nuclear form of uracil-DNA glycosylase, mUNG2, inhibits its activity and causes its degradation. In immunoprecipitation assays the human paralog, hFAM72A, binds hUNG2 and is a potential anti-cancer drug target because of its high expression in many cancers. Using purified mFAM72A, and mUNG2 proteins we show that mFAM72A binds mUNG2, and the N-terminal 25 amino acids of mUNG2 bind mFAM72A at a nanomolar dissociation constant. We also show that mFAM72A is present throughout the cells, and mUNG2 helps localize it to nuclei. Based on in silico models of mFAM72A-mUNG2 interactions, we constructed several mutants of mFAM72A and found that while they have reduced ability to deplete mUNG2, the mutations also destabilized the former protein. We confirmed that Withaferin A, a predicted lead molecule for the design of FAM72A inhibitors, binds mFAM72A with micromolar affinity but has little affinity to mUNG2. We identified two potential metal-binding sites in mFAM72A and show that one of the sites contains an Fe-S cluster. This redox-sensitive cluster is involved in the mFAM72A-mUNG2 interaction and modulates mFAM72A activity. Hydrogen peroxide treatment of cells increases mUNG2 depletion in a FAM72A-dependent fashion suggesting that mFAM72A activity is redox-sensitive.</div>","PeriodicalId":300,"journal":{"name":"DNA Repair","volume":"118 ","pages":"Article 103381"},"PeriodicalIF":3.8,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"3342834","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 1

DNA double-strand break repair in male germ cells during spermatogenesis and its association with male infertility development 精子发生过程中男性生殖细胞DNA双链断裂修复及其与男性不育发展的关系

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-10-01 DOI: 10.1016/j.dnarep.2022.103386

Gunel Talibova, Yesim Bilmez, Saffet Ozturk

{"title":"DNA double-strand break repair in male germ cells during spermatogenesis and its association with male infertility development","authors":"Gunel Talibova, Yesim Bilmez, Saffet Ozturk","doi":"10.1016/j.dnarep.2022.103386","DOIUrl":"https://doi.org/10.1016/j.dnarep.2022.103386","url":null,"abstract":"<div>Spermatogenesis is a complex developmental process. During this process, male germ cells from spermatogonia to sperm cells encounter a number of DNA damages. The most severe form of these damages is double-strand breaks (DSBs) deriving from exogenous and endogenous genotoxic insults. DSBs must be correctly repaired in a short time to maintain genomic integrity in the male germ cells. For this purpose, there are four pathways working in repair of DSBs: homologous recombination (HR), classical non-homologous end joining (cNHEJ), alternative end joining (aEJ), and single strand annealing (SSA). While the HR pathway repairs DSBs with a homology-based and error-free manner, the cNHEJ, aEJ, and SSA pathways join free ends in a sequence-independent mechanism. Possible impairments in these DSB repair mechanisms can lead to cell cycle arrest, abnormal meiotic recombination, and ultimately male infertility. In this review, we comprehensively introduce DSB repair pathways being used by male germ cells during spermatogenesis. Also, potential relationship between dysfunction in these pathways and male infertility development are discussed in the light of existing studies.</div>","PeriodicalId":300,"journal":{"name":"DNA Repair","volume":"118 ","pages":"Article 103386"},"PeriodicalIF":3.8,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"2892970","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

BCLAF1, a functional partner of BACH1, participates in DNA damage response BCLAF1是BACH1的功能伴侣，参与DNA损伤应答

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-10-01 DOI: 10.1016/j.dnarep.2022.103371

Kai Jiang , Yuanyuan Ding , Changjiang Dong , Feifei Shan , Kun Guo , Jiwang Zhang , Feng Zhang

引用次数: 1

Transcription and genome integrity 转录和基因组完整性

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-10-01 DOI: 10.1016/j.dnarep.2022.103373

Mats Ljungman

引用次数: 1

Replication dependent and independent mechanisms of GAA repeat instability GAA重复不稳定性的复制依赖和独立机制

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-10-01 DOI: 10.1016/j.dnarep.2022.103385

Chiara Masnovo, Ayesha F. Lobo, Sergei M. Mirkin

{"title":"Replication dependent and independent mechanisms of GAA repeat instability","authors":"Chiara Masnovo, Ayesha F. Lobo, Sergei M. Mirkin","doi":"10.1016/j.dnarep.2022.103385","DOIUrl":"https://doi.org/10.1016/j.dnarep.2022.103385","url":null,"abstract":"<div>Trinucleotide repeat instability is a driver of human disease. Large expansions of (GAA)n repeats in the first intron of the FXN gene are the cause Friedreich’s ataxia (FRDA), a progressive degenerative disorder which cannot yet be prevented or treated. (GAA)n repeat instability arises during both replication-dependent processes, such as cell division and intergenerational transmission, as well as in terminally differentiated somatic tissues. Here, we provide a brief historical overview on the discovery of (GAA)n repeat expansions and their association to FRDA, followed by recent advances in the identification of triplex H-DNA formation and replication fork stalling. The main body of this review focuses on the last decade of progress in understanding the mechanism of (GAA)n repeat instability during DNA replication and/or DNA repair. We propose that the discovery of additional mechanisms of (GAA)n repeat instability can be achieved via both comparative approaches to other repeat expansion diseases and genome-wide association studies. Finally, we discuss the advances towards FRDA prevention or amelioration that specifically target (GAA)n repeat expansions.</div>","PeriodicalId":300,"journal":{"name":"DNA Repair","volume":"118 ","pages":"Article 103385"},"PeriodicalIF":3.8,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9675320/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"1569154","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

The fast-growing business of Serine ADP-ribosylation 快速发展的丝氨酸adp核糖化业务

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-10-01 DOI: 10.1016/j.dnarep.2022.103382

Edoardo José Longarini , Ivan Matic

引用次数: 8

Review of DNA repair enzymes in bacteria: With a major focus on AddAB and RecBCD 细菌中DNA修复酶的研究进展:重点是AddAB和RecBCD

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-10-01 DOI: 10.1016/j.dnarep.2022.103389

Bing-Bing Wang, Jian-Zhong Xu , Feng Zhang, Shuai Liu, Jie Liu, Wei-Guo Zhang

{"title":"Review of DNA repair enzymes in bacteria: With a major focus on AddAB and RecBCD","authors":"Bing-Bing Wang, Jian-Zhong Xu , Feng Zhang, Shuai Liu, Jie Liu, Wei-Guo Zhang","doi":"10.1016/j.dnarep.2022.103389","DOIUrl":"https://doi.org/10.1016/j.dnarep.2022.103389","url":null,"abstract":"<div>DNA recombination repair systems are essential for organisms to maintain genomic stability. In recent years, we have improved our understanding of the mechanisms of RecBCD/AddAB family-mediated DNA double-strand break repair. In E. coli, it is RecBCD that plays a central role, and in Firmicute Bacillus subtilis it is the AddAB complex that functions. However, there are open questions about the mechanism of DNA repair in bacteria. For example, how bacteria containing crossover hotspot instigator (Chi) sites regulate the activity of proteins. In addition, we still do not know the exact process by which the RecB nuclease or AddA nuclease structural domains load RecA onto DNA. We also know little about the mechanism of DNA repair in the industrially important production bacterium Corynebacterium glutamicum (C. glutamicum). Therefore, exploring DNA repair mechanisms in bacteria may not only deepen our understanding of the DNA repair process in this species but also guide us in the targeted treatment of diseases associated with recombination defects, such as cancer. In this paper, we firstly review the classical proteins RecBCD and AddAB involved in DNA recombination repair, secondly focus on the novel helical nuclease AdnAB found in the genus Mycobacterium.</div>","PeriodicalId":300,"journal":{"name":"DNA Repair","volume":"118 ","pages":"Article 103389"},"PeriodicalIF":3.8,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"1566285","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 1

Roles of phosphatases in eukaryotic DNA replication initiation control 磷酸酶在真核生物DNA复制起始控制中的作用

IF 3.8 3区生物学

DNA Repair Pub Date : 2022-10-01 DOI: 10.1016/j.dnarep.2022.103384

Fiona Jenkinson, Philip Zegerman

引用次数: 0