{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T21:30:57Z","timestamp":1791322257487,"version":"4.3.1"},"reference-count":49,"publisher":"Cold Spring Harbor Laboratory","issue":"19","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Genes Dev."],"published-print":{"date-parts":[[2005,10,1]]},"abstract":"<jats:p>\n                    This paper shows that the small RNA MicA (previously SraD) is an antisense regulator of\n                    <jats:italic>ompA<\/jats:italic>\n                    in\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    . MicA accumulates upon entry into stationary phase and down-regulates the level of\n                    <jats:italic>ompA<\/jats:italic>\n                    mRNA. Regulation of\n                    <jats:italic>ompA<\/jats:italic>\n                    (outer membrane protein A), previously attributed to Hfq\/mRNA binding, is lost upon deletion of the\n                    <jats:italic>micA<\/jats:italic>\n                    gene, whereas overexpression of MicA inhibits the synthesis of OmpA. In vitro, MicA binds to the\n                    <jats:italic>ompA<\/jats:italic>\n                    mRNA leader. Enzymatic and chemical probing was used to map the structures of MicA, the\n                    <jats:italic>ompA<\/jats:italic>\n                    mRNA leader, and the complex formed upon binding. MicA binding generates a footprint across the\n                    <jats:italic>ompA<\/jats:italic>\n                    Shine-Dalgarno sequence, consistent with a 12 + 4 base-pair interaction, which is additionally supported by the effect of mutations in vivo and by bioinformatics analysis of enterobacterial\n                    <jats:italic>micA\/ompA<\/jats:italic>\n                    homolog sequences. MicA is conserved in many enterobacteria, as is its\n                    <jats:italic>ompA<\/jats:italic>\n                    target site. In vitro toeprinting confirmed that binding of MicA specifically interferes with ribosome binding. We propose that MicA, when present at high levels, blocks ribosome binding at the\n                    <jats:italic>ompA<\/jats:italic>\n                    translation start site, which\u2014in line with previous work\u2014secondarily facilitates RNase E cleavage and subsequent mRNA decay. MicA requires the presence of the Hfq protein, although the mechanistic basis for this remains unclear.\n                  <\/jats:p>","DOI":"10.1101\/gad.354405","type":"journal-article","created":{"date-parts":[[2005,10,3]],"date-time":"2005-10-03T18:13:00Z","timestamp":1128363180000},"page":"2355-2366","source":"Crossref","is-referenced-by-count":293,"title":["Hfq-dependent regulation of OmpA synthesis is mediated by an antisense RNA"],"prefix":"10.1101","volume":"19","author":[{"given":"Klas I.","family":"Udekwu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabien","family":"Darfeuille","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J\u00f6rg","family":"Vogel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johan","family":"Reimeg\u00e5rd","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erik","family":"Holmqvist","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E. 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