Lin28a uses distinct mechanisms of binding to RNA and affects miRNA levels positively and negatively
Lin28a inhibits the biogenesis of let-7 miRNAs by triggering the polyuridylation and degradation of their precursors by terminal uridylyltransferases TUT4/7 and 3'-5' exoribonuclease Dis3l2, respectively. Previously, we showed that Lin28a also controls the production of neuro-specific miRN...
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| Veröffentlicht in: | RNA (Cambridge) 2017-03, Vol.23 (3), p.317-332 |
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| creator | Nowak, Jakub Stanislaw Hobor, Fruzsina Downie Ruiz Velasco, Angela Choudhury, Nila Roy Heikel, Gregory Kerr, Alastair Ramos, Andres Michlewski, Gracjan |
| description | Lin28a inhibits the biogenesis of let-7 miRNAs by triggering the polyuridylation and degradation of their precursors by terminal uridylyltransferases TUT4/7 and 3'-5' exoribonuclease Dis3l2, respectively. Previously, we showed that Lin28a also controls the production of neuro-specific miRNA-9 via a polyuridylation-independent mechanism. Here we reveal that the sequences and structural characteristics of pre-let-7 and pre-miRNA-9 are eliciting two distinct modes of binding to Lin28a. We present evidence that Dis3l2 controls miRNA-9 production. Finally, we show that the constitutive expression of untagged Lin28a during neuronal differentiation in vitro positively and negatively affects numerous other miRNAs. Our findings shed light on the role of Lin28a in differentiating cells and on the ways in which one RNA-binding protein can perform multiple roles in the regulation of RNA processing. |
| doi_str_mv | 10.1261/rna.059196.116 |
| format | Article |
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Previously, we showed that Lin28a also controls the production of neuro-specific miRNA-9 via a polyuridylation-independent mechanism. Here we reveal that the sequences and structural characteristics of pre-let-7 and pre-miRNA-9 are eliciting two distinct modes of binding to Lin28a. We present evidence that Dis3l2 controls miRNA-9 production. Finally, we show that the constitutive expression of untagged Lin28a during neuronal differentiation in vitro positively and negatively affects numerous other miRNAs. Our findings shed light on the role of Lin28a in differentiating cells and on the ways in which one RNA-binding protein can perform multiple roles in the regulation of RNA processing.</description><identifier>ISSN: 1355-8382</identifier><identifier>EISSN: 1469-9001</identifier><identifier>DOI: 10.1261/rna.059196.116</identifier><identifier>PMID: 27881476</identifier><language>eng</language><publisher>United States: Cold Spring Harbor Laboratory Press</publisher><subject>Animals ; Base Pairing ; Base Sequence ; Cell Differentiation - drug effects ; Cell Line, Tumor ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Exoribonucleases - genetics ; Exoribonucleases - metabolism ; Gene Expression Regulation ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; HeLa Cells ; Humans ; Mice ; MicroRNAs - genetics ; MicroRNAs - metabolism ; Neurons - cytology ; Neurons - drug effects ; Neurons - metabolism ; Nucleic Acid Conformation ; Pluripotent Stem Cells - cytology ; Pluripotent Stem Cells - drug effects ; Pluripotent Stem Cells - metabolism ; Poly U - metabolism ; Protein Binding ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; RNA Cleavage ; RNA Nucleotidyltransferases - genetics ; RNA Nucleotidyltransferases - metabolism ; RNA Precursors - genetics ; RNA Precursors - metabolism ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Tretinoin - pharmacology</subject><ispartof>RNA (Cambridge), 2017-03, Vol.23 (3), p.317-332</ispartof><rights>2017 Nowak et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society.</rights><rights>2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-7daff5de7b94eaa217abec24808803fdb690f777adaf6b85715b4fee2dc12b253</citedby><cites>FETCH-LOGICAL-c423t-7daff5de7b94eaa217abec24808803fdb690f777adaf6b85715b4fee2dc12b253</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5311490/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5311490/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27881476$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nowak, Jakub Stanislaw</creatorcontrib><creatorcontrib>Hobor, Fruzsina</creatorcontrib><creatorcontrib>Downie Ruiz Velasco, Angela</creatorcontrib><creatorcontrib>Choudhury, Nila Roy</creatorcontrib><creatorcontrib>Heikel, Gregory</creatorcontrib><creatorcontrib>Kerr, Alastair</creatorcontrib><creatorcontrib>Ramos, Andres</creatorcontrib><creatorcontrib>Michlewski, Gracjan</creatorcontrib><title>Lin28a uses distinct mechanisms of binding to RNA and affects miRNA levels positively and negatively</title><title>RNA (Cambridge)</title><addtitle>RNA</addtitle><description>Lin28a inhibits the biogenesis of let-7 miRNAs by triggering the polyuridylation and degradation of their precursors by terminal uridylyltransferases TUT4/7 and 3'-5' exoribonuclease Dis3l2, respectively. 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Hobor, Fruzsina ; Downie Ruiz Velasco, Angela ; Choudhury, Nila Roy ; Heikel, Gregory ; Kerr, Alastair ; Ramos, Andres ; Michlewski, Gracjan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-7daff5de7b94eaa217abec24808803fdb690f777adaf6b85715b4fee2dc12b253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>Base Pairing</topic><topic>Base Sequence</topic><topic>Cell Differentiation - drug effects</topic><topic>Cell Line, Tumor</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Exoribonucleases - genetics</topic><topic>Exoribonucleases - metabolism</topic><topic>Gene Expression Regulation</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Mice</topic><topic>MicroRNAs - genetics</topic><topic>MicroRNAs - metabolism</topic><topic>Neurons - cytology</topic><topic>Neurons - drug effects</topic><topic>Neurons - metabolism</topic><topic>Nucleic Acid Conformation</topic><topic>Pluripotent Stem Cells - cytology</topic><topic>Pluripotent Stem Cells - drug effects</topic><topic>Pluripotent Stem Cells - metabolism</topic><topic>Poly U - metabolism</topic><topic>Protein Binding</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>RNA Cleavage</topic><topic>RNA Nucleotidyltransferases - genetics</topic><topic>RNA Nucleotidyltransferases - metabolism</topic><topic>RNA Precursors - genetics</topic><topic>RNA Precursors - metabolism</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Tretinoin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nowak, Jakub Stanislaw</creatorcontrib><creatorcontrib>Hobor, Fruzsina</creatorcontrib><creatorcontrib>Downie Ruiz Velasco, Angela</creatorcontrib><creatorcontrib>Choudhury, Nila Roy</creatorcontrib><creatorcontrib>Heikel, Gregory</creatorcontrib><creatorcontrib>Kerr, Alastair</creatorcontrib><creatorcontrib>Ramos, Andres</creatorcontrib><creatorcontrib>Michlewski, Gracjan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Nucleic Acids Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>RNA (Cambridge)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nowak, Jakub Stanislaw</au><au>Hobor, Fruzsina</au><au>Downie Ruiz Velasco, Angela</au><au>Choudhury, Nila Roy</au><au>Heikel, Gregory</au><au>Kerr, Alastair</au><au>Ramos, Andres</au><au>Michlewski, Gracjan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lin28a uses distinct mechanisms of binding to RNA and affects miRNA levels positively and negatively</atitle><jtitle>RNA (Cambridge)</jtitle><addtitle>RNA</addtitle><date>2017-03</date><risdate>2017</risdate><volume>23</volume><issue>3</issue><spage>317</spage><epage>332</epage><pages>317-332</pages><issn>1355-8382</issn><eissn>1469-9001</eissn><abstract>Lin28a inhibits the biogenesis of let-7 miRNAs by triggering the polyuridylation and degradation of their precursors by terminal uridylyltransferases TUT4/7 and 3'-5' exoribonuclease Dis3l2, respectively. 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| ispartof | RNA (Cambridge), 2017-03, Vol.23 (3), p.317-332 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals Base Pairing Base Sequence Cell Differentiation - drug effects Cell Line, Tumor DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Exoribonucleases - genetics Exoribonucleases - metabolism Gene Expression Regulation Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism HeLa Cells Humans Mice MicroRNAs - genetics MicroRNAs - metabolism Neurons - cytology Neurons - drug effects Neurons - metabolism Nucleic Acid Conformation Pluripotent Stem Cells - cytology Pluripotent Stem Cells - drug effects Pluripotent Stem Cells - metabolism Poly U - metabolism Protein Binding Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RNA Cleavage RNA Nucleotidyltransferases - genetics RNA Nucleotidyltransferases - metabolism RNA Precursors - genetics RNA Precursors - metabolism RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Tretinoin - pharmacology |
| title | Lin28a uses distinct mechanisms of binding to RNA and affects miRNA levels positively and negatively |
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