{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T19:46:39Z","timestamp":1760298399329},"reference-count":33,"publisher":"American Society for Microbiology","issue":"19","license":[{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"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":[[2011,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The 23S rRNA gene of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Coxiella burnetii<\/jats:named-content>\n            , the agent of Q fever in humans, contains an unusually high number of conserved, selfish genetic elements, including two group I introns, termed Cbu.L1917 (L1917) and Cbu.L1951 (L1951). To better understand the role that introns play in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Coxiella<\/jats:named-content>\n            's biology, we determined the intrinsic stability time periods (\n            <jats:italic>in vitro<\/jats:italic>\n            half-lives) of the encoded ribozymes to be \u223c15 days for L1917 and \u223c5 days for L1951, possibly due to differences in their sizes (551 and 1,559 bases, respectively), relative degrees of compactness of the respective RNA structures, and amounts of single-stranded RNA.\n            <jats:italic>In vivo<\/jats:italic>\n            half-lives for both introns were also determined to be \u223c11 min by the use of RNase protection assays and an\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n            model. Intron RNAs were quantified in synchronous cultures of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">C. burnetii<\/jats:named-content>\n            and found to closely parallel those of 16S rRNA; i.e., ribozyme levels significantly increased between days 0 and 3 and then remained stable until 8 days postinfection. Both 16S rRNA and ribozyme levels fell during the stationary and death phases (days 8 to 14). The marked stability of the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Coxiella<\/jats:named-content>\n            intron RNAs is presumably conferred by their association with ribosomes, a stoichiometric relationship that was determined to be one ribozyme, of either type, per 500 ribosomes. Inaccuracies in splicing (exon 2 skipping) were found to increase during the first 5 days in culture, with a rate of approximately one improperly spliced 23S rRNA per 1.3 million copies. The\n            <jats:italic>in vitro<\/jats:italic>\n            efficiency of L1917 intron splicing was significantly enhanced in the presence of a recombinant\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Coxiella<\/jats:named-content>\n            RNA DEAD-box helicase (CBU_0670) relative to that of controls, suggesting that this enzyme may serve as an intron RNA splice facilitator\n            <jats:italic>in vivo<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/jb.05472-11","type":"journal-article","created":{"date-parts":[[2011,7,30]],"date-time":"2011-07-30T04:50:36Z","timestamp":1312001436000},"page":"5292-5299","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":7,"title":["Ribozyme Stability, Exon Skipping, and a Potential Role for RNA Helicase in Group I Intron Splicing by Coxiella burnetii"],"prefix":"10.1128","volume":"193","author":[{"given":"Linda D.","family":"Hicks","sequence":"first","affiliation":[{"name":"Division of Biological Sciences, The University of Montana, Missoula, Montana 59812"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Indu","family":"Warrier","sequence":"additional","affiliation":[{"name":"Division of Biological Sciences, The University of Montana, Missoula, Montana 59812"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rahul","family":"Raghavan","sequence":"additional","affiliation":[{"name":"Department of Ecology and Evolutionary Biology, Yale University, New Haven, Connecticut 06520"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael F.","family":"Minnick","sequence":"additional","affiliation":[{"name":"Division of Biological Sciences, The University of Montana, Missoula, Montana 59812"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.177.10.2946-2949.1995"},{"key":"e_1_3_2_3_2","volume-title":"Current protocols in molecular biology.","author":"Ausubel F. 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