{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T15:07:16Z","timestamp":1792076836630,"version":"4.4.0"},"reference-count":71,"publisher":"Oxford University Press (OUP)","issue":"16","license":[{"start":{"date-parts":[[2024,7,30]],"date-time":"2024-07-30T00:00:00Z","timestamp":1722297600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI093569"],"award-info":[{"award-number":["AI093569"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI146172"],"award-info":[{"award-number":["AI146172"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,9,9]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Non-segmented negative-strand (NNS) RNA viruses, such as rabies, Nipah\u00a0and Ebola, produce 5\u2032-capped and 3\u2032-polyadenylated mRNAs resembling higher eukaryotic mRNAs. Here, we developed a transcription elongation-coupled pre-mRNA capping system for vesicular stomatitis virus (VSV, a prototypic NNS RNA virus). Using this system, we demonstrate that the single-polypeptide RNA-dependent RNA polymerase (RdRp) large protein (L) catalyzes all pre-mRNA modifications co-transcriptionally in the following order: (i) 5\u2032-capping (polyribonucleotidylation of GDP) to form a GpppA cap core structure, (ii) 2\u2032-O-methylation of GpppA into GpppAm, (iii) guanine-N7-methylation of GpppAm into m7GpppAm (cap 1), (iv) 3\u2032-polyadenylation to yield a poly(A) tail. The GDP polyribonucleotidyltransferase (PRNTase) domain of L generated capped pre-mRNAs of 18 nucleotides or longer via the formation of covalent enzyme\u2013pre-mRNA intermediates. The single methyltransferase domain of L sequentially methylated the cap structure only when pre-mRNAs of 40 nucleotides or longer were associated with elongation complexes. These results suggest that the formation of pre-mRNA closed loop structures in elongation complexes via the RdRp and PRNTase domains followed by the RdRp and MTase domains on the same polypeptide is required for the cap 1 formation during transcription. Taken together, our findings indicate that NNS RNA virus L acts as an all-in-one viral mRNA assembly machinery.<\/jats:p>","DOI":"10.1093\/nar\/gkae659","type":"journal-article","created":{"date-parts":[[2024,7,30]],"date-time":"2024-07-30T20:08:02Z","timestamp":1722370082000},"page":"9803-9820","source":"Crossref","is-referenced-by-count":8,"title":["The complete pathway for co-transcriptional mRNA maturation within a large protein of a non-segmented negative-strand RNA virus"],"prefix":"10.1093","volume":"52","author":[{"given":"Minako","family":"Ogino","sequence":"first","affiliation":[{"name":"Department of Medical Microbiology and Immunology, College of Medicine and Life Sciences, University of Toledo , Toledo , OH 43614 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Todd\u00a0J","family":"Green","sequence":"additional","affiliation":[{"name":"Department of Microbiology, School of Medicine, University of Alabama at Birmingham , Birmingham , AL 35294 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4154-1781","authenticated-orcid":false,"given":"Tomoaki","family":"Ogino","sequence":"additional","affiliation":[{"name":"Department of Medical Microbiology and Immunology, College of Medicine and Life Sciences, University of Toledo , Toledo , OH 43614 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,7,30]]},"reference":[{"key":"2024090903592509000_B1","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1073\/pnas.80.5.1251","article-title":"Promoter-proximal pausing by RNA polymerase II in vitro: transcripts shorter than 20 nucleotides are not capped","volume":"80","author":"Coppola","year":"1983","journal-title":"Proc. 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Chem."},{"key":"2024090903592509000_B10","doi-asserted-by":"crossref","first-page":"e0193804","DOI":"10.1371\/journal.pone.0193804","article-title":"2\u2032-O-methylation of the mRNA cap protects RNAs from decapping and degradation by DXO","volume":"13","author":"Picard-Jean","year":"2018","journal-title":"PLoS One"},{"key":"2024090903592509000_B11","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1038\/nature09489","article-title":"2\u2032-O methylation of the viral mRNA cap evades host restriction by IFIT family members","volume":"468","author":"Daffis","year":"2010","journal-title":"Nature"},{"key":"2024090903592509000_B12","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1038\/ni.1979","article-title":"Ribose 2\u2032-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5","volume":"12","author":"Zust","year":"2011","journal-title":"Nat. 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Acad. Sci. U.S.A."},{"key":"2024090903592509000_B33","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1099\/vir.0.019307-0","article-title":"The HR motif in the RNA-dependent RNA polymerase L protein of Chandipura virus is required for unconventional mRNA-capping activity","volume":"91","author":"Ogino","year":"2010","journal-title":"J. Gen. Virol."},{"key":"2024090903592509000_B34","doi-asserted-by":"crossref","first-page":"144","DOI":"10.3390\/v8050144","article-title":"The rabies virus L protein catalyzes mRNA capping with GDP polyribonucleotidyltransferase activity","volume":"8","author":"Ogino","year":"2016","journal-title":"Viruses"},{"key":"2024090903592509000_B35","doi-asserted-by":"crossref","first-page":"7237","DOI":"10.1016\/S0021-9258(18)34562-9","article-title":"RNA capping by HeLa cell RNA guanylyltransferase. Characterization of a covalent protein-guanylate intermediate","volume":"257","author":"Shuman","year":"1982","journal-title":"J. Biol. 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