{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T21:51:26Z","timestamp":1781214686768,"version":"3.54.1"},"reference-count":35,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2001,12,25]],"date-time":"2001-12-25T00:00:00Z","timestamp":1009238400000},"content-version":"vor","delay-in-days":450,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Plant Journal"],"published-print":{"date-parts":[[2000,10]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>DNA helicases play an essential role in all aspects of nucleic acid metabolism, by providing a duplex\u2010unwinding function. This is the first report of the isolation of a cDNA (1.6\u2003kb) clone encoding functional DNA helicase from a plant (pea, <jats:italic>Pisum sativum<\/jats:italic>). The deduced amino\u2010acid sequence has eight conserved helicase motifs of the DEAD\u2010box protein family. It is a unique member of this family, containing DESD and SRT motifs instead of DEAD\/H and SAT. The encoded 45.5\u2003kDa protein has been overexpressed in bacteria and purified to homogeneity. The purified protein contains ATP\u2010dependent DNA and RNA helicase, DNA\u2010dependent ATPase, and ATP\u2010binding activities. The protein sequence contains striking homology with eIF\u20104A, which has not so far been reported as DNA helicase. The antibodies against pea helicase inhibit <jats:italic>in vitro<\/jats:italic> translation. The gene is expressed as 1.6\u2003kb mRNA in different organs of pea. The enzyme is localized in the nucleus and cytosol, and unwinds DNA in the 3\u2032 to 5\u2032 direction. The pea helicase interacts with pea topoisomerase I protein and stimulates its activity. These results suggest that pea DNA helicase could be an important multifunctional protein involved in protein synthesis, maintaining the basic activities of the cell, and in upregulation of topoisomerase I activity. The discovery of such a protein with intrinsic multiple activity should make an important contribution to our better understanding of DNA and RNA transactions in plants.<\/jats:p>","DOI":"10.1046\/j.1365-313x.2000.00869.x","type":"journal-article","created":{"date-parts":[[2003,3,12]],"date-time":"2003-03-12T22:01:56Z","timestamp":1047506516000},"page":"219-229","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":74,"title":["A DNA helicase from <i>Pisum sativum<\/i> is homologous to translation initiation factor and stimulates topoisomerase I activity"],"prefix":"10.1111","volume":"24","author":[{"given":"Xuan Hoi","family":"Pham","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Malireddy Kodandarami","family":"Reddy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nasreen Z.","family":"Ehtesham","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bharati","family":"Matta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Narendra","family":"Tuteja","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2001,12,25]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/27.2.628"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.4.1993"},{"key":"e_1_2_5_4_1","first-page":"545","volume-title":"DNA Replication in Eukaryotic Cells","author":"Borowiec J.A.","year":"1996"},{"key":"e_1_2_5_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.17.7642"},{"key":"e_1_2_5_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(85)91096-4"},{"key":"e_1_2_5_7_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1993.tb01173.x"},{"key":"e_1_2_5_8_1","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1093\/nar\/11.5.1475","article-title":"Accurate transcription initiation by RNA polymerase II in a soluble extract from mammalian nuclei","volume":"11","author":"Dignam J.D.","year":"1983","journal-title":"Nucl. 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