{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T07:40:09Z","timestamp":1773301209566,"version":"3.50.1"},"reference-count":35,"publisher":"American Society for Microbiology","issue":"16","license":[{"start":{"date-parts":[[2003,8,15]],"date-time":"2003-08-15T00:00:00Z","timestamp":1060905600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2003,8,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The\n            <jats:italic>Neisseria gonorrhoeae<\/jats:italic>\n            genome encodes a homologue of the\n            <jats:italic>Escherichia coli<\/jats:italic>\n            FNR protein (the fumarate and nitrate reductase regulator). Despite its similarity to\n            <jats:italic>E. coli<\/jats:italic>\n            FNR, the gonococcal FNR only partially complemented an\n            <jats:italic>E. coli fnr<\/jats:italic>\n            mutation. After error-prone PCR mutagenesis of the gonococcal\n            <jats:italic>fnr<\/jats:italic>\n            gene, we identified four mutant\n            <jats:italic>fnr<\/jats:italic>\n            derivatives carrying the same S18F substitution, and we showed that the mutant FNR could activate transcription from a range of class I and class II FNR-dependent promoters in\n            <jats:italic>E. coli<\/jats:italic>\n            . Prompted by the similarities between gonococcal and\n            <jats:italic>E. coli<\/jats:italic>\n            FNR, we made changes in gonococcal\n            <jats:italic>fnr<\/jats:italic>\n            that created substitutions that are equivalent to previously characterized substitutions in\n            <jats:italic>E. coli<\/jats:italic>\n            FNR. First, our experiments showed that cysteine, C116, in the gonococcal FNR, equivalent to C122 in\n            <jats:italic>E. coli<\/jats:italic>\n            FNR, is essential, presumably because, as in\n            <jats:italic>E. coli<\/jats:italic>\n            FNR, it binds to an iron-sulfur center. Second, the L22H and D148A substitutions in gonococcal FNR were made. These changes are equivalent to the L28H and D154A changes in\n            <jats:italic>E. coli<\/jats:italic>\n            FNR, which had been shown to increase FNR activity in the presence of oxygen. We show that the effects of these substitutions in gonococcal FNR are distinct from those of the S18F substitution. Similarly, substitutions in the putative activating regions of gonococcal FNR were made. We show that the activity of gonococcal FNR in\n            <jats:italic>E. coli<\/jats:italic>\n            can be increased by transplanting certain activating regions from\n            <jats:italic>E. coli<\/jats:italic>\n            FNR. The effects of these substitutions are additive to those due to S18F. From these data, we conclude that the effects of the S18F substitution in gonococcal FNR are distinct from the effects of the other substitutions. S18 is immediately adjacent to one of three N-terminal cysteine residues that coordinate the iron-sulfur center, and thus the S18F substitution is most likely to stabilize this center. Support for this came from complementary experiments in which we created the S24F substitution in\n            <jats:italic>E. coli<\/jats:italic>\n            FNR, which is equivalent to the S18F substitution in gonococcal FNR. Our results show that the S24F substitution changes the activity of\n            <jats:italic>E. coli<\/jats:italic>\n            FNR and that the changes are distinct from those due to previously characterized substitutions.\n          <\/jats:p>","DOI":"10.1128\/jb.185.16.4734-4747.2003","type":"journal-article","created":{"date-parts":[[2003,8,1]],"date-time":"2003-08-01T23:08:04Z","timestamp":1059779284000},"page":"4734-4747","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":10,"title":["Transcription Activation at\n            <i>Escherichia coli<\/i>\n            FNR-Dependent Promoters by the Gonococcal FNR Protein: Effects of a Novel S18F Substitution and Comparisons with the Corresponding Substitution in\n            <i>E. coli<\/i>\n            FNR"],"prefix":"10.1128","volume":"185","author":[{"given":"Tim","family":"Overton","sequence":"first","affiliation":[{"name":"School of Biosciences, University of Birmingham, Birmingham B15 2TT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eleanor G. F.","family":"Reid","sequence":"additional","affiliation":[{"name":"School of Biosciences, University of Birmingham, Birmingham B15 2TT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robin","family":"Foxall","sequence":"additional","affiliation":[{"name":"School of Biosciences, University of Birmingham, Birmingham B15 2TT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Harry","family":"Smith","sequence":"additional","affiliation":[{"name":"School of Biosciences, University of Birmingham, Birmingham B15 2TT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen J. W.","family":"Busby","sequence":"additional","affiliation":[{"name":"School of Biosciences, University of Birmingham, Birmingham B15 2TT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jeffrey A.","family":"Cole","sequence":"additional","affiliation":[{"name":"School of Biosciences, University of Birmingham, Birmingham B15 2TT, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"6234","DOI":"10.1074\/jbc.275.9.6234","volume":"275","year":"2000","unstructured":"Bates, D. M., C. V. Popescu, N. Khoroshilova, K. Vogt, H. Beinert, E. M\u00fcnck, and P. J. Kiley. 2000. Substitution of leucine 28 with a histidine in the Escherichia coli transcription factor FNR results in increased stability of the [4Fe-4S]2+ cluster to oxygen. J. Biol. Chem.275:6234-6240.","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"3865","DOI":"10.1093\/nar\/17.10.3865","volume":"17","year":"1989","unstructured":"Bell, A., K. L. Gaston, J. A. Cole, and S. J. W. Busby. 1989. Cloning of binding sequences for the Escherichia coli transcription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRP. Nucleic Acids Res.17:3865-3874.","journal-title":"Nucleic Acids Res."},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.184.21.5855-5861.2002"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1046\/j.1365-2958.2002.02776.x","volume":"43","year":"2002","unstructured":"Browning, D. F., C. M. Beatty, A. J. Wolfe, J. A. Cole, and S. J. Busby. 2002. Independent regulation of the divergent Escherichia coli nrfA and acsP1 promoters by a nucleoprotein assembly at a shared regulatory region. Mol. Microbiol.43:687-701.","journal-title":"Mol. Microbiol."},{"key":"e_1_3_2_6_2","unstructured":"Browning D. F. D. Lee J. Green and S. J. Busby. 2002. Secrets of bacterial transcription initiation taught by the Escherichia coli FNR protein p. 127-142. In D. A. Hodgson and C. M. Thomas (ed.) Signals switches regulons and cascades: control of bacterial gene expression. Proceedings of the 150th ordinary meeting. Society for General Microbiology Reading United Kingdom."},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1006\/jmbi.1999.3161","volume":"293","year":"1999","unstructured":"Busby, S. J. W., and R. H. Ebright. 1999. Transcription activation by catabolite activator protein (CAP). J. Mol. Biol.293:199-213.","journal-title":"J. Mol. Biol."},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.55.6.1359-1364.1987"},{"key":"e_1_3_2_9_2","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/0882-4010(88)90038-1","volume":"5","year":"1988","unstructured":"Clark, V. L., J. S. 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