PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs
Messenger RNAs produced by splicing are translated more efficiently than those produced from similar intronless precursor mRNAs (pre-mRNAs). The exon-junction complex (EJC) probably mediates this enhancement; however, the specific link between the EJC and the translation machinery has not been ident...
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| Veröffentlicht in: | Nature structural & molecular biology 2007-12, Vol.14 (12), p.1173-1179 |
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| creator | Diem, Michael D Chan, Chia C Younis, Ihab Dreyfuss, Gideon |
| description | Messenger RNAs produced by splicing are translated more efficiently than those produced from similar intronless precursor mRNAs (pre-mRNAs). The exon-junction complex (EJC) probably mediates this enhancement; however, the specific link between the EJC and the translation machinery has not been identified. The EJC proteins Y14 and magoh remain bound to spliced mRNAs after their export from the nucleus to the cytoplasm and are removed only when these mRNAs are translated. Here we show that PYM, a 29-kDa protein that binds the Y14–magoh complex in the cytoplasm, also binds, via a separate domain, to the small (40S) ribosomal subunit and the 48S preinitiation complex. Furthermore, PYM knockdown reduces the translation efficiency of a reporter protein produced from intron-containing, but not intronless, pre-mRNA. We suggest that PYM functions as a bridge between EJC-bearing spliced mRNAs and the translation machinery to enhance translation of the mRNAs. |
| doi_str_mv | 10.1038/nsmb1321 |
| format | Article |
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Academic</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Diem, Michael D</au><au>Chan, Chia C</au><au>Younis, Ihab</au><au>Dreyfuss, Gideon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2007-12-01</date><risdate>2007</risdate><volume>14</volume><issue>12</issue><spage>1173</spage><epage>1179</epage><pages>1173-1179</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Messenger RNAs produced by splicing are translated more efficiently than those produced from similar intronless precursor mRNAs (pre-mRNAs). The exon-junction complex (EJC) probably mediates this enhancement; however, the specific link between the EJC and the translation machinery has not been identified. The EJC proteins Y14 and magoh remain bound to spliced mRNAs after their export from the nucleus to the cytoplasm and are removed only when these mRNAs are translated. Here we show that PYM, a 29-kDa protein that binds the Y14–magoh complex in the cytoplasm, also binds, via a separate domain, to the small (40S) ribosomal subunit and the 48S preinitiation complex. Furthermore, PYM knockdown reduces the translation efficiency of a reporter protein produced from intron-containing, but not intronless, pre-mRNA. We suggest that PYM functions as a bridge between EJC-bearing spliced mRNAs and the translation machinery to enhance translation of the mRNAs.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>18026120</pmid><doi>10.1038/nsmb1321</doi><tpages>7</tpages></addata></record> |
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| subjects | Biochemistry Biological Microscopy Biomedical and Life Sciences Carrier Proteins - metabolism Cell Line Cytoplasm - metabolism Exons Genetic engineering Humans Immunoprecipitation Life Sciences Membrane Biology Messenger RNA Molecular biology Physiological aspects Protein Binding Protein Biosynthesis Protein Structure Proteins Ribonucleic acid Ribosomes - metabolism RNA RNA Splicing RNA, Messenger - genetics Structure |
| title | PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs |
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