Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex
Mammalian mRNA biogenesis requires specific recognition of a hexanucleotide AAUAAA motif in the polyadenylation signals (PAS) of precursor mRNA (pre-mRNA) transcripts by the cleavage and polyadenylation specificity factor (CPSF) complex. Here we present a 3.1-Å-resolution cryo-EM structure of a core...
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| Veröffentlicht in: | Nature structural & molecular biology 2018-02, Vol.25 (2), p.135-138 |
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| creator | Clerici, Marcello Faini, Marco Muckenfuss, Lena M. Aebersold, Ruedi Jinek, Martin |
| description | Mammalian mRNA biogenesis requires specific recognition of a hexanucleotide AAUAAA motif in the polyadenylation signals (PAS) of precursor mRNA (pre-mRNA) transcripts by the cleavage and polyadenylation specificity factor (CPSF) complex. Here we present a 3.1-Å-resolution cryo-EM structure of a core CPSF module bound to the PAS hexamer motif. The structure reveals the molecular interactions responsible for base-specific recognition, providing a rationale for mechanistic differences between mammalian and yeast 3′ polyadenylation.
The cryo-EM structure of the human core CPSF complex, containing CPSF160, WDR33, CPSF30 and Fip1 subunits, bound to its RNA target reveals the mechanism of PAS recognition. |
| doi_str_mv | 10.1038/s41594-017-0020-6 |
| format | Article |
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The cryo-EM structure of the human core CPSF complex, containing CPSF160, WDR33, CPSF30 and Fip1 subunits, bound to its RNA target reveals the mechanism of PAS recognition.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/s41594-017-0020-6</identifier><identifier>PMID: 29358758</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/337/1645/2570 ; 631/45/500 ; 631/45/535/1258 ; Amino Acid Motifs ; Biochemistry ; Biological Microscopy ; Biological research ; Biomedical and Life Sciences ; Biosynthesis ; Brief Communication ; Cells (Biology) ; Cleavage And Polyadenylation Specificity Factor - chemistry ; Cryoelectron Microscopy ; Genetic aspects ; Humans ; Hydrogen bonds ; Image Processing, Computer-Assisted ; Life Sciences ; Mammals ; Membrane Biology ; Messenger RNA ; Molecular biology ; Molecular interactions ; Molecular Structure ; Motion ; Nuclear Proteins - chemistry ; Poly A - chemistry ; Polyadenylation ; Polypeptides ; Protein Binding ; Protein Domains ; Protein Multimerization ; Protein Structure ; Recognition ; RNA ; RNA Precursors - chemistry ; RNA, Messenger - chemistry ; Structure ; Transcription (Genetics) ; Yeast ; Yeasts</subject><ispartof>Nature structural & molecular biology, 2018-02, Vol.25 (2), p.135-138</ispartof><rights>The Author(s) 2018</rights><rights>COPYRIGHT 2018 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Feb 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c637t-da1484a3b5f6e5bd035818795f79b85aae212764646f99685cc0b0199b64877d3</citedby><cites>FETCH-LOGICAL-c637t-da1484a3b5f6e5bd035818795f79b85aae212764646f99685cc0b0199b64877d3</cites><orcidid>0000-0002-7601-210X ; 0000-0002-9576-3267 ; 0000-0003-2906-0982</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41594-017-0020-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41594-017-0020-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29358758$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Clerici, Marcello</creatorcontrib><creatorcontrib>Faini, Marco</creatorcontrib><creatorcontrib>Muckenfuss, Lena M.</creatorcontrib><creatorcontrib>Aebersold, Ruedi</creatorcontrib><creatorcontrib>Jinek, Martin</creatorcontrib><title>Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Mammalian mRNA biogenesis requires specific recognition of a hexanucleotide AAUAAA motif in the polyadenylation signals (PAS) of precursor mRNA (pre-mRNA) transcripts by the cleavage and polyadenylation specificity factor (CPSF) complex. Here we present a 3.1-Å-resolution cryo-EM structure of a core CPSF module bound to the PAS hexamer motif. The structure reveals the molecular interactions responsible for base-specific recognition, providing a rationale for mechanistic differences between mammalian and yeast 3′ polyadenylation.
The cryo-EM structure of the human core CPSF complex, containing CPSF160, WDR33, CPSF30 and Fip1 subunits, bound to its RNA target reveals the mechanism of PAS recognition.</description><subject>631/337/1645/2570</subject><subject>631/45/500</subject><subject>631/45/535/1258</subject><subject>Amino Acid Motifs</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biological research</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Brief Communication</subject><subject>Cells (Biology)</subject><subject>Cleavage And Polyadenylation Specificity Factor - chemistry</subject><subject>Cryoelectron Microscopy</subject><subject>Genetic aspects</subject><subject>Humans</subject><subject>Hydrogen bonds</subject><subject>Image Processing, Computer-Assisted</subject><subject>Life Sciences</subject><subject>Mammals</subject><subject>Membrane Biology</subject><subject>Messenger RNA</subject><subject>Molecular biology</subject><subject>Molecular interactions</subject><subject>Molecular Structure</subject><subject>Motion</subject><subject>Nuclear Proteins - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Clerici, Marcello</au><au>Faini, Marco</au><au>Muckenfuss, Lena M.</au><au>Aebersold, Ruedi</au><au>Jinek, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2018-02-01</date><risdate>2018</risdate><volume>25</volume><issue>2</issue><spage>135</spage><epage>138</epage><pages>135-138</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Mammalian mRNA biogenesis requires specific recognition of a hexanucleotide AAUAAA motif in the polyadenylation signals (PAS) of precursor mRNA (pre-mRNA) transcripts by the cleavage and polyadenylation specificity factor (CPSF) complex. Here we present a 3.1-Å-resolution cryo-EM structure of a core CPSF module bound to the PAS hexamer motif. The structure reveals the molecular interactions responsible for base-specific recognition, providing a rationale for mechanistic differences between mammalian and yeast 3′ polyadenylation.
The cryo-EM structure of the human core CPSF complex, containing CPSF160, WDR33, CPSF30 and Fip1 subunits, bound to its RNA target reveals the mechanism of PAS recognition.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>29358758</pmid><doi>10.1038/s41594-017-0020-6</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-7601-210X</orcidid><orcidid>https://orcid.org/0000-0002-9576-3267</orcidid><orcidid>https://orcid.org/0000-0003-2906-0982</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 631/337/1645/2570 631/45/500 631/45/535/1258 Amino Acid Motifs Biochemistry Biological Microscopy Biological research Biomedical and Life Sciences Biosynthesis Brief Communication Cells (Biology) Cleavage And Polyadenylation Specificity Factor - chemistry Cryoelectron Microscopy Genetic aspects Humans Hydrogen bonds Image Processing, Computer-Assisted Life Sciences Mammals Membrane Biology Messenger RNA Molecular biology Molecular interactions Molecular Structure Motion Nuclear Proteins - chemistry Poly A - chemistry Polyadenylation Polypeptides Protein Binding Protein Domains Protein Multimerization Protein Structure Recognition RNA RNA Precursors - chemistry RNA, Messenger - chemistry Structure Transcription (Genetics) Yeast Yeasts |
| title | Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex |
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