{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang H"],"funding":["National Program on Key Research Project of China","Key research and Development Program of Hangzhou","Zhejiang Provincial Natural Science Foundation of China","Scientific Research Fund of Zhejiang Provincial Education Department","Zhejiang Provincial Key R&amp;D Program","Horizon 2020 - Research and Innovation Framework Programme","Zhejiang Provincial Key R&D Program"],"pagination":["RP95648"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11221836"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["Bacterial exonuclease III (ExoIII), widely acknowledged for specifically targeting double-stranded DNA (dsDNA), has been documented as a DNA repair-associated nuclease with apurinic/apyrimidinic (AP)-endonuclease and 3'→5' exonuclease activities. Due to these enzymatic properties, ExoIII has been broadly applied in molecular biosensors. Here, we demonstrate that ExoIII (<i>Escherichia coli</i>) possesses highly active enzymatic activities on ssDNA. By using a range of ssDNA fluorescence-quenching reporters and fluorophore-labeled probes coupled with mass spectrometry analysis, we found ExoIII cleaved the ssDNA at 5'-bond of phosphodiester from 3' to 5' end by both exonuclease and endonuclease activities. Additional point mutation analysis identified the critical residues for the ssDNase ac"],"journal":["eLife"],"pubmed_title":["Bacterial exonuclease III expands its enzymatic activities on single-stranded DNA."],"pmcid":["PMC11221836"],"funding_grant_id":["2019YFE0103900","LZ24C180002","202203A08","2022YFC2604201","861917-SAFFI","Y202250872","2021C02008","2023C03045"],"pubmed_authors":["Jiang Z","Li Y","Ye C","Zhou C","Zhao G","Jiang C","Yue M","Wang H","Zhang C","Lu Q","Li N"],"additional_accession":[]},"is_claimable":false,"name":"Bacterial exonuclease III expands its enzymatic activities on single-stranded DNA.","description":"Bacterial exonuclease III (ExoIII), widely acknowledged for specifically targeting double-stranded DNA (dsDNA), has been documented as a DNA repair-associated nuclease with apurinic/apyrimidinic (AP)-endonuclease and 3'→5' exonuclease activities. Due to these enzymatic properties, ExoIII has been broadly applied in molecular biosensors. Here, we demonstrate that ExoIII (<i>Escherichia coli</i>) possesses highly active enzymatic activities on ssDNA. By using a range of ssDNA fluorescence-quenching reporters and fluorophore-labeled probes coupled with mass spectrometry analysis, we found ExoIII cleaved the ssDNA at 5'-bond of phosphodiester from 3' to 5' end by both exonuclease and endonuclease activities. Additional point mutation analysis identified the critical residues for the ssDNase ac","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-02T21:18:39.759Z","creation":"2025-04-04T12:21:38.49Z"},"accession":"S-EPMC11221836","cross_references":{"pubmed":["38959062"],"doi":["10.7554/eLife.95648"]}}