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Chinese Academy of Sciences Institutional Repositories Grid
Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains

文献类型:期刊论文

作者Ariza, Antonio6,7; Liu, Qiang3,4,5; Cowieson, Nathan P.2; Ahel, Ivan6; Filippov, Dmitri V.5; Rack, Johannes Gregor Matthias1
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
出版日期2024-10-01
卷号300期号:10页码:20
DOI10.1016/j.jbc.2024.107770
通讯作者Ahel, Ivan(ivan.ahel@path.ox.ac.uk) ; Filippov, Dmitri V.(lippov@lic.leidenuniv.nl) ; Rack, Johannes Gregor Matthias(j.rack@exeter.ac.uk)
英文摘要Dynamic ADP-ribosylation signaling is a crucial pathway that controls fundamental cellular processes, in particular, the response to cellular stresses such as DNA damage, reactive oxygen species, and infection. In some pathogenic microbes, the response to oxidative stress is controlled by a SirTM/zinccontaining macrodomain (Zn-Macro) pair responsible for establishment and removal of the modification, respectively. Targeting this defence mechanism against the host's innate immune response may lead to novel approaches to support the fight against emerging antimicrobial resistance. Earlier studies suggested that Zn-Macros play a key role in the activation of this defence. Therefore, we used phylogenetic, biochemical, and structural approaches to elucidate the functional properties of these enzymes. Using the substrate mimetic asparagineADP-ribose as well as the ADP-ribose product, we characterize the catalytic role of the zinc ion in the removal of the ADPribosyl modification. Furthermore, we determined structural properties that contribute to substrate selectivity within the different Zn-Macro branches. Together, our data not only give new insights into the Zn-Macro family but also highlight their distinct features that may be exploited for the development of future therapies.
WOS关键词MULTIPLE SEQUENCE ALIGNMENT ; GLYCINE CLEAVAGE SYSTEM ; ANGLE SCATTERING DATA ; REACTION-MECHANISM ; PROTEIN ; IDENTIFICATION ; COORDINATION ; EXPRESSION ; SOFTWARE ; DOMAINS
资助项目MRC Centre for Medical Mycology at the University of Exeter[MR/N006364/2] ; MRC Centre for Medical Mycology at the University of Exeter[MR/V033417/1] ; NIHR Exeter Biomedical Research Centre ; China Scholarship Council (CSC) ; Wellcome Trust[210634] ; Wellcome Trust[223107] ; Biotechnology and Biological Sciences Research Council[BB/R007195/1] ; Biotechnology and Biological Sciences Research Council[BB/W016613/1] ; Cancer Research United Kingdom[C35050/A22284] ; Medical Research Council[MR/X007472/1]
WOS研究方向Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:001331651300001
出版者ELSEVIER
源URL[http://119.78.100.183/handle/2S10ELR8/313802]  
专题中国科学院上海药物研究所
通讯作者Ahel, Ivan; Filippov, Dmitri V.; Rack, Johannes Gregor Matthias
作者单位1.Univ Exeter, Med Res Council Ctr Med Mycol, Exeter, England
2.Harwell Sci & Innovat Campus, Diamond Light Source, Didcot, Oxon, England
3.Chinese Acad Sci, Shanghai Inst Mat Med, Beijing, Peoples R China
4.Chinese Acad Sci, Shanghai Inst Mat Med, Zhongshan Inst Drug Discovery, Beijing, Peoples R China
5.Leiden Univ, Leiden Inst Chem, Bioorgan Synth, Leiden, Netherlands
6.Univ Oxford, Sir William Dunn Sch Pathol, Oxford, England
7.Univ Sheffield, Sch Biosci, Sheffield, England
推荐引用方式
GB/T 7714
Ariza, Antonio,Liu, Qiang,Cowieson, Nathan P.,et al. Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2024,300(10):20.
APA Ariza, Antonio,Liu, Qiang,Cowieson, Nathan P.,Ahel, Ivan,Filippov, Dmitri V.,&Rack, Johannes Gregor Matthias.(2024).Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains.JOURNAL OF BIOLOGICAL CHEMISTRY,300(10),20.
MLA Ariza, Antonio,et al."Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains".JOURNAL OF BIOLOGICAL CHEMISTRY 300.10(2024):20.

入库方式: OAI收割

来源:上海药物研究所

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