{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T21:04:56Z","timestamp":1791493496653,"version":"4.3.4"},"reference-count":70,"publisher":"Oxford University Press (OUP)","issue":"13","license":[{"start":{"date-parts":[[2021,3,23]],"date-time":"2021-03-23T00:00:00Z","timestamp":1616457600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"DFG","doi-asserted-by":"publisher","award":["Fi573\/7-2"],"award-info":[{"award-number":["Fi573\/7-2"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"DFG","doi-asserted-by":"publisher","award":["8-2"],"award-info":[{"award-number":["8-2"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"name":"DAAD-STIBET"},{"DOI":"10.13039\/100007393","name":"Association Fran\u00e7aise contre les Myopathies","doi-asserted-by":"publisher","award":["21656"],"award-info":[{"award-number":["21656"]}],"id":[{"id":"10.13039\/100007393","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,7,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>The macromolecular SMN complex facilitates the formation of Sm-class ribonucleoproteins involved in mRNA processing (UsnRNPs). While biochemical studies have revealed key activities of the SMN complex, its structural investigation is lagging behind. Here we report on the identification and structural determination of the SMN complex from the lower eukaryote Schizosaccharomyces pombe, consisting of SMN, Gemin2, 6, 7, 8\u00a0and Sm proteins. The core of the SMN complex is formed by several copies of SMN tethered through its C-terminal alpha-helices arranged with alternating polarity. This creates a central platform onto which Gemin8 binds and recruits Gemins 6 and 7. The N-terminal parts of the SMN molecules extrude via flexible linkers from the core and enable binding of Gemin2 and Sm proteins. Our data identify the SMN complex as a multivalent hub where Sm proteins are collected in its periphery to allow their joining with UsnRNA.<\/jats:p>","DOI":"10.1093\/nar\/gkab158","type":"journal-article","created":{"date-parts":[[2021,2,26]],"date-time":"2021-02-26T12:24:04Z","timestamp":1614342244000},"page":"7207-7223","source":"Crossref","is-referenced-by-count":13,"title":["Identification and structural analysis of the <i>Schizosaccharomyces pombe<\/i> SMN complex"],"prefix":"10.1093","volume":"49","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9757-1595","authenticated-orcid":false,"given":"Jyotishman","family":"Veepaschit","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Biocenter, University of W\u00fcrzburg, W\u00fcrzburg\u00a097074, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7640-9406","authenticated-orcid":false,"given":"Aravindan","family":"Viswanathan","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Biocenter, University of W\u00fcrzburg, W\u00fcrzburg\u00a097074, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1445-5802","authenticated-orcid":false,"given":"R\u00e9my","family":"Bordonn\u00e9","sequence":"additional","affiliation":[{"name":"Institut de G\u00e9n\u00e9tique Mol\u00e9culaire de Montpellier, University of Montpellier, CNRS, Montpellier\u00a034293, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9085-5130","authenticated-orcid":false,"given":"Clemens","family":"Grimm","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Biocenter, University of W\u00fcrzburg, W\u00fcrzburg\u00a097074, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1465-6591","authenticated-orcid":false,"given":"Utz","family":"Fischer","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Biocenter, University of W\u00fcrzburg, W\u00fcrzburg\u00a097074, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2021,3,23]]},"reference":[{"key":"2021071913025937300_B1","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1016\/j.cell.2009.02.009","article-title":"The spliceosome: design principles of a dynamic RNP machine","volume":"136","author":"Wahl","year":"2009","journal-title":"Cell"},{"key":"2021071913025937300_B2","doi-asserted-by":"crossref","first-page":"a003707","DOI":"10.1101\/cshperspect.a003707","article-title":"Spliceosome structure and function","volume":"3","author":"Will","year":"2011","journal-title":"Cold Spring Harbor Perspect. 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Cell Biol."},{"key":"2021071913025937300_B6","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1007\/s00412-017-0637-6","article-title":"UsnRNP biogenesis: mechanisms and regulation","volume":"126","author":"Gruss","year":"2017","journal-title":"Chromosoma"},{"key":"2021071913025937300_B7","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1002\/j.1460-2075.1996.tb00579.x","article-title":"The snRNP core assembly pathway: identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro","volume":"15","author":"Raker","year":"1996","journal-title":"EMBO J."},{"key":"2021071913025937300_B8","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/S0092-8674(00)80550-4","article-title":"Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs","volume":"96","author":"Kambach","year":"1999","journal-title":"Cell"},{"key":"2021071913025937300_B9","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/35054102","article-title":"Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle","volume":"409","author":"Stark","year":"2001","journal-title":"Nature"},{"key":"2021071913025937300_B10","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1093\/emboj\/20.1.187","article-title":"Sm protein\u2013Sm site RNA interactions within the inner ring of the spliceosomal snRNP core structure","volume":"20","author":"Urlaub","year":"2001","journal-title":"EMBO J."},{"key":"2021071913025937300_B11","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1126\/science.2143847","article-title":"An essential signaling role for the m3G cap in the transport of U1 snRNP to the nucleus","volume":"249","author":"Fischer","year":"1990","journal-title":"Science"},{"key":"2021071913025937300_B12","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/0092-8674(90)90292-M","article-title":"Monomethylated cap structures facilitate RNA export from the nucleus","volume":"63","author":"Hamm","year":"1990","journal-title":"Cell"},{"key":"2021071913025937300_B13","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1016\/S1097-2765(02)00484-7","article-title":"Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus","volume":"9","author":"Mouaikel","year":"2002","journal-title":"Mol. cell"},{"key":"2021071913025937300_B14","doi-asserted-by":"crossref","first-page":"4899","DOI":"10.1093\/nar\/gkg656","article-title":"Sequence\u2013structure\u2013function relationships of Tgs1, the yeast snRNA\/snoRNA cap hypermethylase","volume":"31","author":"Mouaikel","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"2021071913025937300_B15","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1016\/S0960-9822(99)80475-8","article-title":"Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway","volume":"9","author":"Sleeman","year":"1999","journal-title":"Curr. 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