{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T09:59:27Z","timestamp":1790416767490,"version":"4.1.0"},"reference-count":47,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T00:00:00Z","timestamp":1790380800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T00:00:00Z","timestamp":1790380800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001411","name":"Indian Council of Medical Research","doi-asserted-by":"publisher","award":["EMDR\/SG\/14\/2023\u20104164"],"award-info":[{"award-number":["EMDR\/SG\/14\/2023\u20104164"]}],"id":[{"id":"10.13039\/501100001411","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>\n                    RecQ helicases are ubiquitous genome maintenance proteins that can resolve complex DNA structures during replication, recombination, and repair. Eukaryotic RecQ helicases are known to interact with replication protein A (RPA), leading to the stimulation of their unwinding activity. In higher eukaryotes, this interaction is mediated through the acidic residues of RecQ helicases and the N\u2010terminal OB fold (DBD\u2010F) of RPA70. In kinetoplastid parasites, the RPA70 homolog lacks this N\u2010terminal DBD\u2010F domain, raising the possibility of alternative interaction mechanisms. Here, we investigate the physical and functional interaction between the catalytic core of RECQb helicase and RPA1 from\n                    <jats:italic>Leishmania donovani<\/jats:italic>\n                    parasite. Using molecular docking, GST pull\u2010down assays, and Surface Plasmon Resonance analysis (SPR), we demonstrate that the winged\u2010helix (WH) domain of LdRECQb interacts with the C\u2010terminal OB fold 3 (OBF3) of LdRPA1, unraveling a non\u2010conventional interaction mechanism. Functional assays reveal that LdRPA1 stimulates LdRECQb_heli (catalytic core) unwinding activity on long DNA duplexes, Holliday junctions, and G\u2010quadruplex structures without affecting its ATP hydrolysis. Deletion of the OBF3 drastically reduces but does not abolish this stimulatory effect completely. Our results suggest that while OBF3 predominantly interacts with the LdRECQb, other OB folds of RPA1 may also contribute to this stimulatory effect. Furthermore, we demonstrate that the LdRECQb\u2010LdRPA1 association facilitates restoration of model\u2010regressed replication forks\n                    <jats:italic>in vitro<\/jats:italic>\n                    , suggesting a conserved role in replication stress response. Our results reveal a new C\u2010terminus\u2010mediated RPA\u2010RecQ interaction in\n                    <jats:italic>L.\u00a0donovani<\/jats:italic>\n                    that resembles the prokaryotic SSB\u2010RecQ interaction mechanism, while maintaining functional conservation of eukaryotic DNA metabolism.\n                  <\/jats:p>","DOI":"10.1111\/febs.70742","type":"journal-article","created":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T09:31:31Z","timestamp":1790415091000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Replication protein\n                    <scp>A1<\/scp>\n                    from\n                    <i>L. donovani<\/i>\n                    interacts with\n                    <scp>RECQb<\/scp>\n                    via the C\u2010terminal\n                    <scp>OB<\/scp>\n                    fold and stimulates its helicase activity on branched substrates"],"prefix":"10.1111","author":[{"given":"Mayukh","family":"Chakraborty","sequence":"first","affiliation":[{"name":"Department of Bioscience and Biotechnology Indian Institute of Technology Kharagpur  India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susmita","family":"Ghosh","sequence":"additional","affiliation":[{"name":"Department of Bioscience and Biotechnology Indian Institute of Technology Kharagpur  India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Surasree","family":"Chakraborty","sequence":"additional","affiliation":[{"name":"Department of Bioscience and Biotechnology Indian Institute of Technology Kharagpur  India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Riya","family":"Ajmera","sequence":"additional","affiliation":[{"name":"Department of Bioscience and Biotechnology Indian Institute of Technology Kharagpur  India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarbartha","family":"Mukherjee","sequence":"additional","affiliation":[{"name":"Department of Bioscience and Biotechnology Indian Institute of Technology Kharagpur  India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arif Uj","family":"Jaman","sequence":"additional","affiliation":[{"name":"Department of Bioscience and Biotechnology Indian Institute of Technology Kharagpur  India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4172-071X","authenticated-orcid":false,"given":"Agneyo","family":"Ganguly","sequence":"additional","affiliation":[{"name":"Department of Bioscience and Biotechnology Indian Institute of Technology Kharagpur  India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,26]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"publisher","DOI":"10.1007\/978\u20101\u20104614\u20105037\u20105_8"},{"key":"e_1_2_10_3_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev\u2010biochem\u2010060713\u2010035428"},{"key":"e_1_2_10_4_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/cdg500"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI147301"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkg398"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.str.2005.04.018"},{"key":"e_1_2_10_8_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0806908106"},{"key":"e_1_2_10_9_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkq1031"},{"key":"e_1_2_10_10_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1416746112"},{"key":"e_1_2_10_11_1","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/B978-0-12-814685-9.00005-1","volume-title":"Helicases 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