{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,31]],"date-time":"2025-12-31T20:02:58Z","timestamp":1767211378816,"version":"3.48.0"},"reference-count":49,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,11,4]],"date-time":"2025-11-04T00:00:00Z","timestamp":1762214400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004731","name":"Zhejiang Province Natural Science Foundation","doi-asserted-by":"publisher","award":["LDQ23C050002"],"award-info":[{"award-number":["LDQ23C050002"]}],"id":[{"id":"10.13039\/501100004731","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32222001"],"award-info":[{"award-number":["32222001"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32170028"],"award-info":[{"award-number":["32170028"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2025,12]]},"DOI":"10.1016\/j.ijbiomac.2025.148652","type":"journal-article","created":{"date-parts":[[2025,10,30]],"date-time":"2025-10-30T00:09:59Z","timestamp":1761782999000},"page":"148652","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"P2","title":["Phosphorylation of RecA at the Loop 1 region modulates its activity in response to DNA damage"],"prefix":"10.1016","volume":"332","author":[{"given":"Jing","family":"Hu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuchen","family":"Cao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jingli","family":"Dai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bing","family":"Tian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Liangyan","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuejin","family":"Hua","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ye","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2025.148652_bb0005","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20225678","article-title":"Goals and challenges in bacterial phosphoproteomics","volume":"20","author":"Yague","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0010","doi-asserted-by":"crossref","first-page":"270","DOI":"10.3389\/fgene.2014.00270","article-title":"Physicochemical mechanisms of protein regulation by phosphorylation","volume":"5","author":"Nishi","year":"2014","journal-title":"Front. Genet."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0015","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/j.tibs.2005.04.013","article-title":"Protein phosphorylation in signaling--50 years and counting","volume":"30","author":"Pawson","year":"2005","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0020","doi-asserted-by":"crossref","first-page":"3638","DOI":"10.1021\/pr100150w","article-title":"Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis","volume":"9","author":"Soufi","year":"2010","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0025","doi-asserted-by":"crossref","first-page":"5481","DOI":"10.1021\/pr200762y","article-title":"Phosphoproteome analysis of Streptomyces development reveals extensive protein phosphorylation accompanying bacterial differentiation","volume":"10","author":"Manteca","year":"2011","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0030","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1074\/mcp.M700311-MCP200","article-title":"Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser\/Thr\/Tyr phosphorylation","volume":"7","author":"Macek","year":"2008","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0035","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2021.637836","article-title":"Identification and phenotypic characterization of Hsp90 phosphorylation sites that modulate virulence traits in the major human fungal pathogen Candida albicans","volume":"11","author":"Alaalm","year":"2021","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0040","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.51620","article-title":"An atypical DYRK kinase connects quorum-sensing with posttranscriptional gene regulation in Trypanosoma brucei","volume":"9","author":"Cayla","year":"2020","journal-title":"Elife"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0045","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00128-19","article-title":"Phosphorylation of human papillomavirus type 16 L2 contributes to efficient virus infectious entry","volume":"93","author":"Broniarczyk","year":"2019","journal-title":"J. Virol."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0050","doi-asserted-by":"crossref","first-page":"184","DOI":"10.3389\/fmicb.2016.00184","article-title":"Role of protein phosphorylation in the regulation of cell cycle and DNA-related processes in bacteria","volume":"7","author":"Garcia-Garcia","year":"2016","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0055","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1093\/femsre\/fuy037","article-title":"Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species","volume":"43","author":"Lim","year":"2019","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0060","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.csbj.2016.04.001","article-title":"A decade of biochemical and structural studies of the DNA repair machinery of Deinococcus radiodurans: major findings, functional and mechanistic insight and challenges","volume":"14","author":"Timmins","year":"2016","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0065","doi-asserted-by":"crossref","first-page":"2810","DOI":"10.1016\/j.csbj.2020.09.036","article-title":"Structural features and functional implications of proteins enabling the robustness of Deinococcus radiodurans","volume":"18","author":"Chen","year":"2020","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0070","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/nrmicro2073","article-title":"A new perspective on radiation resistance based on Deinococcus radiodurans","volume":"7","author":"Daly","year":"2009","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0075","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0012570","article-title":"Small-molecule antioxidant proteome-shields in Deinococcus radiodurans","volume":"5","author":"Daly","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0080","doi-asserted-by":"crossref","DOI":"10.1016\/j.micres.2020.126559","article-title":"Late embryogenesis abundant group3 protein (DrLEA3) is involved in antioxidation in the extremophilic bacterium Deinococcus radiodurans","volume":"240","author":"Dai","year":"2020","journal-title":"Microbiol. Res."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0085","doi-asserted-by":"crossref","first-page":"5550","DOI":"10.1093\/nar\/gkv444","article-title":"Structural insights into catalysis and dimerization enhanced exonuclease activity of RNase","volume":"43","author":"Zhao","year":"2015","journal-title":"J. Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0090","doi-asserted-by":"crossref","first-page":"9925","DOI":"10.1093\/nar\/gkz720","article-title":"Structure and DNA damage-dependent derepression mechanism for the XRE family member DG-DdrO","volume":"47","author":"Lu","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0095","doi-asserted-by":"crossref","DOI":"10.1002\/pmic.201900158","article-title":"Succinylome analysis reveals the involvement of lysine succinylation in the extreme resistance of Deinococcus radiodurans","volume":"19","author":"Zhou","year":"2019","journal-title":"Proteomics"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0100","article-title":"Lysine acetylome profiling reveals diverse functions of acetylation in Deinococcus radiodurans","volume":"10","author":"Zhang","year":"2022","journal-title":"Microbiol. Spectr."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0105","article-title":"New Insights into radio-resistance mechanism revealed by (phospho)proteome analysis of Deinococcus Radiodurans after heavy ion irradiation","volume":"24","author":"Liu","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0110","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/nrmicro2917","article-title":"Bacterial DNA repair: recent insights into the mechanism of RecBCD, AddAB and AdnAB","volume":"11","author":"Wigley","year":"2013","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0115","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1042\/BST20190558","article-title":"RecA and DNA recombination: a review of molecular mechanisms","volume":"47","author":"Del Val","year":"2019","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0120","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1073\/pnas.53.2.451","article-title":"Isolation and characterization of recombination-deficient mutants of Escherichia Coli K12","volume":"53","author":"Clark","year":"1965","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0125","doi-asserted-by":"crossref","DOI":"10.1038\/nature06971","article-title":"Mechanism of homologous recombination from the RecA-ssDNA\/dsDNA structures","volume":"453","author":"Chen","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0130","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1016\/j.ijbiomac.2022.07.176","article-title":"Interaction of RecA mediated SOS response with bacterial persistence, biofilm formation, and host response","volume":"217","author":"Kaushik","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0135","doi-asserted-by":"crossref","DOI":"10.3390\/cells10040924","article-title":"Coexistence of SOS-dependent and SOS-independent regulation of DNA repair genes in radiation-resistant Deinococcus bacteria","volume":"10","author":"Blanchard","year":"2021","journal-title":"Cells"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0140","doi-asserted-by":"crossref","first-page":"7917","DOI":"10.1073\/pnas.122218499","article-title":"The RecA proteins of Deinococcus radiodurans and Escherichia coli promote DNA strand exchange via inverse pathways","volume":"99","author":"Kim","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0145","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.dnarep.2015.05.002","article-title":"Enhanced DNA binding affinity of RecA protein from Deinococcus radiodurans","volume":"31","author":"Warfel","year":"2015","journal-title":"DNA Repair (Amst)"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0150","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.bbrc.2015.09.042","article-title":"Deinococcus radiodurans RecA nucleoprotein filaments characterized at the single-molecule level with optical tweezers","volume":"466","author":"Pobegalov","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0155","doi-asserted-by":"crossref","first-page":"21351","DOI":"10.1074\/jbc.M113.459230","article-title":"Regulation of Deinococcus radiodurans RecA protein function via modulation of active and inactive nucleoprotein filament states","volume":"288","author":"Ngo","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0160","doi-asserted-by":"crossref","first-page":"16672","DOI":"10.1074\/jbc.M116.736389","article-title":"Phosphorylation of Deinococcus radiodurans RecA regulates its activity and may contribute to radioresistance","volume":"291","author":"Rajpurohit","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0165","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/j.jmb.2004.09.087","article-title":"Crystal structure of RecA from Deinococcus radiodurans: insights into the structural basis of extreme radioresistance","volume":"344","author":"Rajan","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0170","doi-asserted-by":"crossref","first-page":"1892","DOI":"10.1038\/s41467-024-46208-9","article-title":"The Deinococcus protease PprI senses DNA damage by directly interacting with single-stranded DNA","volume":"15","author":"Lu","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0175","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.01144-24","article-title":"cAMP-independent DNA binding of the CRP family protein DdrI from Deinococcus radiodurans","volume":"15","author":"Wang","year":"2024","journal-title":"mBio"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0180","article-title":"Cyclic AMP receptor protein acts as a transcription regulator in response to stresses in Deinococcus radiodurans","volume":"11","author":"Yang","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0185","doi-asserted-by":"crossref","DOI":"10.1128\/JB.00129-18","article-title":"DdrI, a cAMP receptor protein family member, acts as a major regulator for adaptation of Deinococcus radiodurans to various stresses","volume":"200","author":"Meyer","year":"2018","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0190","doi-asserted-by":"crossref","DOI":"10.3389\/fgene.2021.632423","article-title":"MazEF toxin-antitoxin system-mediated DNA damage stress response in Deinococcus radiodurans","volume":"12","author":"Dai","year":"2021","journal-title":"Front. Genet."},{"issue":"1233\u20131241","key":"10.1016\/j.ijbiomac.2025.148652_bb0195","article-title":"The ribosomal protein uL22 modulates the shape of the protein exit tunnel","volume":"25","author":"Wekselman","year":"2017","journal-title":"Structure"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0200","doi-asserted-by":"crossref","first-page":"891","DOI":"10.2174\/0929866529666220819121911","article-title":"Phosphorylation regulation of a histone-like HU protein from Deinococcus radiodurans","volume":"29","author":"Hou","year":"2022","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0205","doi-asserted-by":"crossref","first-page":"6406","DOI":"10.1093\/nar\/gkae379","article-title":"Stress-induced nucleoid remodeling in Deinococcus radiodurans is associated with major changes in Heat Unstable (HU) protein dynamics","volume":"52","author":"Vauclare","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0210","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1111\/mmi.12233","article-title":"Bacillus subtilis serine\/threonine protein kinase YabT is involved in spore development via phosphorylation of a bacterial recombinase","volume":"88","author":"Bidnenko","year":"2013","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0215","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1093\/nar\/gku1364","article-title":"Loop L1 governs the DNA-binding specificity and order for RecA-catalyzed reactions in homologous recombination and DNA repair","volume":"43","author":"Shinohara","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0220","doi-asserted-by":"crossref","first-page":"9510","DOI":"10.1093\/nar\/gky748","article-title":"The ATPase activity of E. coli RecA prevents accumulation of toxic complexes formed by erroneous binding to undamaged double stranded DNA","volume":"46","author":"Gataulin","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0225","doi-asserted-by":"crossref","DOI":"10.1128\/msphere.00412-22","article-title":"ATPase activity of Bacillus subtilis RecA affects the dynamic formation of RecA filaments at DNA double strand breaks","volume":"7","author":"Hernandez-Tamayo","year":"2022","journal-title":"mSphere"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0230","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.01322","article-title":"Evolution of extreme resistance to ionizing radiation via genetic adaptation of DNA repair","volume":"3","author":"Byrne","year":"2014","journal-title":"Elife"},{"issue":"152\u2013161","key":"10.1016\/j.ijbiomac.2025.148652_bb0235","article-title":"Mycobacterial mutagenesis and drug resistance are controlled by phosphorylation- and cardiolipin-mediated inhibition of the RecA coprotease","volume":"72","author":"Wipperman","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0240","doi-asserted-by":"crossref","first-page":"11315","DOI":"10.1093\/nar\/gky911","article-title":"Structural basis of 5\u2032 flap recognition and protein-protein interactions of human flap endonuclease 1","volume":"46","author":"Xu","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2025.148652_bb0245","doi-asserted-by":"crossref","first-page":"9266","DOI":"10.1038\/s41467-024-53641-3","article-title":"Hop2-Mnd1 functions as a DNA sequence fidelity switch in Dmc1-mediated DNA recombination","volume":"15","author":"Peng","year":"2024","journal-title":"Nat. Commun."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025092098?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025092098?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,12,31]],"date-time":"2025-12-31T19:55:05Z","timestamp":1767210905000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813025092098"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12]]},"references-count":49,"alternative-id":["S0141813025092098"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.148652","relation":{},"ISSN":["0141-8130"],"issn-type":[{"type":"print","value":"0141-8130"}],"subject":[],"published":{"date-parts":[[2025,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Phosphorylation of RecA at the Loop 1 region modulates its activity in response to DNA damage","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.148652","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"148652"}}