{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T16:33:00Z","timestamp":1773678780055,"version":"3.50.1"},"reference-count":36,"publisher":"Proceedings of the National Academy of Sciences","issue":"29","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2005,7,19]]},"abstract":"<jats:p>\n            DNA helicases catalyze separation of double-helical DNA into its complementary single strands, a process essential for DNA replication, recombination, and repair. The\n            <jats:italic>Escherichia coli<\/jats:italic>\n            Rep protein, a superfamily 1 DNA helicase, functions in DNA replication restart and is required for replication of several bacteriophages. Monomers of Rep do not display helicase activity\n            <jats:italic>in vitro<\/jats:italic>\n            ; in fact, DNA unwinding requires Rep dimerization. Here we show that removal of the 2B subdomain of Rep to form Rep\u03942B activates monomer helicase activity, albeit with limited processivity. Although both full length Rep and Rep\u03942B monomers can translocate with 3\u2032 to 5\u2032 directionality along single-stranded DNA, the 2B subdomain inhibits the helicase activity of full length Rep. This suggests an autoregulatory mechanism for Rep helicase, which may apply to other nonhexameric helicases, whereby helicase activity is regulated by the rotational conformational state of the 2B subdomain; formation of a Rep dimer may relieve autoinhibition by altering the 2B subdomain orientation.\n          <\/jats:p>","DOI":"10.1073\/pnas.0502886102","type":"journal-article","created":{"date-parts":[[2005,7,12]],"date-time":"2005-07-12T00:34:18Z","timestamp":1121128458000},"page":"10076-10081","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":133,"title":["Autoinhibition of\n            <i>Escherichia coli<\/i>\n            Rep monomer helicase activity by its 2B subdomain"],"prefix":"10.1073","volume":"102","author":[{"given":"Katherine M.","family":"Brendza","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110"}]},{"given":"Wei","family":"Cheng","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110"}]},{"given":"Christopher J.","family":"Fischer","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110"}]},{"given":"Marla A.","family":"Chesnik","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110"}]},{"given":"Anita","family":"Niedziela-Majka","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110"}]},{"given":"Timothy M.","family":"Lohman","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110"}]}],"member":"341","published-online":{"date-parts":[[2005,7,11]]},"reference":[{"key":"e_1_3_2_1_2","doi-asserted-by":"publisher","DOI":"10.1002\/bies.950160103"},{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1017\/S0033583502003864"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.65.070196.001125"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrc1012"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0047-6374(02)00039-8"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.genom.1.1.409"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-440X(05)80116-2"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.69.1.651"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2001.4758"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(02)01276-7"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature02704"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.232401899"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80716-3"},{"key":"e_1_3_2_14_2","first-page":"304","volume":"23","year":"2004","unstructured":"Lohman, T., Hsieh, J., Maluf, N. K., Cheng, W., Lucius, A. L., Fischer, C. J., Brendza, K. M., Korolev, S. & Waksman, G. (2004) in The Enzymes, eds. Hackney, D. D. & Tamanoi, F. (Elsevier Academic, New York), Vol. 23, pp. 304-364.","journal-title":"The Enzymes"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1098\/rstb.2003.1366"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.57.3.813"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature01083"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80525-5"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1038\/384379a0"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/19.14.3799"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.242479399"},{"key":"e_1_3_2_22_2","unstructured":"Cheng W. 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