{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,8]],"date-time":"2026-03-08T06:35:35Z","timestamp":1772951735751,"version":"3.50.1"},"reference-count":62,"publisher":"eLife Sciences Publications, Ltd","license":[{"start":{"date-parts":[[2021,3,19]],"date-time":"2021-03-19T00:00:00Z","timestamp":1616112000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2021,3,19]],"date-time":"2021-03-19T00:00:00Z","timestamp":1616112000000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2021,3,19]],"date-time":"2021-03-19T00:00:00Z","timestamp":1616112000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 GM120353"],"award-info":[{"award-number":["R01 GM120353"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35 GM131704"],"award-info":[{"award-number":["R35 GM131704"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elifesciences.org"],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>\n                    Helicases utilize nucleotide triphosphate (NTP) hydrolysis to translocate along single-stranded nucleic acids (NA) and unwind the duplex. In the cell, helicases function in the context of other NA-associated proteins such as single-stranded DNA binding proteins. Such encounters regulate helicase function, although the underlying mechanisms remain largely unknown.\n                    <jats:italic>Ferroplasma acidarmanus<\/jats:italic>\n                    xeroderma pigmentosum group D (XPD) helicase serves as a model for understanding the molecular mechanisms of superfamily 2B helicases, and its activity is enhanced by the cognate single-stranded DNA binding protein replication protein A 2 (RPA2). Here, optical trap measurements of the unwinding activity of a single XPD helicase in the presence of RPA2 reveal a mechanism in which XPD interconverts between two states with different processivities and transient RPA2 interactions stabilize the more processive state, activating a latent \u2018processivity switch\u2019 in XPD. A point mutation at a regulatory DNA binding site on XPD similarly activates this switch. These findings provide new insights on mechanisms of helicase regulation by accessory proteins.\n                  <\/jats:p>","DOI":"10.7554\/elife.60515","type":"journal-article","created":{"date-parts":[[2021,3,19]],"date-time":"2021-03-19T09:00:20Z","timestamp":1616144420000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.60515","source":"Crossref","is-referenced-by-count":12,"title":["Switch-like control of helicase processivity by single-stranded DNA binding protein"],"prefix":"10.7554","volume":"10","author":[{"given":"Barbara","family":"Stekas","sequence":"first","affiliation":[{"name":"Department of Physics, University of Illinois, Urbana-Champaign, Urbana, United States"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Steve","family":"Yeo","sequence":"additional","affiliation":[{"name":"Center for Biophysics and Quantitative Biology, University of Illinois, Urbana-Champaign, Urbana, United 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