Lsm proteins bind and stabilize RNAs containing 5′ poly(A) tracts
Many orthopoxvirus messenger RNAs have an unusual nontemplated poly(A) tract of 5 to 40 residues at the 5' end. The precise function of this feature is unknown. Here we show that 5' poly(A) tracts are able to repress RNA decay by inhibiting 3'-to-5' exonucleases as well as decapp...
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| Veröffentlicht in: | Nature structural & molecular biology 2007-09, Vol.14 (9), p.824-831 |
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| container_title | Nature structural & molecular biology |
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| creator | Bergman, Naomi Anderson, John R Schneider, Robert J Kambach, Christian Moraes, Karen C M Wilusz, Carol J Wilusz, Jeffrey Zaric, Bozidarka |
| description | Many orthopoxvirus messenger RNAs have an unusual nontemplated poly(A) tract of 5 to 40 residues at the 5' end. The precise function of this feature is unknown. Here we show that 5' poly(A) tracts are able to repress RNA decay by inhibiting 3'-to-5' exonucleases as well as decapping of RNA substrates. UV cross-linking analysis demonstrated that the Lsm complex associates with the 5' poly(A) tract. Furthermore, recombinant Lsm1-7 complex specifically binds 5' poly(A) tracts 10 to 21 nucleotides in length, consistent with the length of 5' poly(A) required for stabilization. Knockdown of Lsm1 abrogates RNA stabilization by the 5' poly(A) tract. We propose that the Lsm complex simultaneously binds the 3' and 5' ends of these unusual messenger RNAs and thereby prevents 3'-to-5' decay. The implications of this phenomenon for cellular mRNA decay are discussed. |
| doi_str_mv | 10.1038/nsmb1287 |
| format | Article |
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The precise function of this feature is unknown. Here we show that 5' poly(A) tracts are able to repress RNA decay by inhibiting 3'-to-5' exonucleases as well as decapping of RNA substrates. UV cross-linking analysis demonstrated that the Lsm complex associates with the 5' poly(A) tract. Furthermore, recombinant Lsm1-7 complex specifically binds 5' poly(A) tracts 10 to 21 nucleotides in length, consistent with the length of 5' poly(A) required for stabilization. Knockdown of Lsm1 abrogates RNA stabilization by the 5' poly(A) tract. We propose that the Lsm complex simultaneously binds the 3' and 5' ends of these unusual messenger RNAs and thereby prevents 3'-to-5' decay. The implications of this phenomenon for cellular mRNA decay are discussed.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb1287</identifier><identifier>PMID: 17694069</identifier><language>eng</language><publisher>United States: Nature Publishing Group</publisher><subject>Animals ; Base Sequence ; Binding proteins ; Cell Line ; Cricetinae ; Crosslinking ; Decay ; DNA Primers ; Genetic aspects ; Genetic recombination ; Genetic translation ; LSm proteins ; Membrane Proteins - metabolism ; Messenger RNA ; Molecular biology ; mRNA turnover ; Nucleotides ; Orthopoxvirus ; Physiological aspects ; Poly A - metabolism ; Polyadenine ; Protein Binding ; Proteins ; Recombinant Proteins - metabolism ; Ribonucleic acid ; RNA ; RNA - chemistry ; RNA - metabolism ; Stabilization ; Substrates ; Ultraviolet Rays ; Viruses</subject><ispartof>Nature structural & molecular biology, 2007-09, Vol.14 (9), p.824-831</ispartof><rights>COPYRIGHT 2007 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Sep 2007</rights><rights>Springer Nature America, Inc. 2007.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525t-1965b5570cb6b55b735f280c0f3c1d144a53af506e09e560169118a2651c335f3</citedby><cites>FETCH-LOGICAL-c525t-1965b5570cb6b55b735f280c0f3c1d144a53af506e09e560169118a2651c335f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,2729,27931,27932</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17694069$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bergman, Naomi</creatorcontrib><creatorcontrib>Anderson, John R</creatorcontrib><creatorcontrib>Schneider, Robert J</creatorcontrib><creatorcontrib>Kambach, Christian</creatorcontrib><creatorcontrib>Moraes, Karen C M</creatorcontrib><creatorcontrib>Wilusz, Carol J</creatorcontrib><creatorcontrib>Wilusz, Jeffrey</creatorcontrib><creatorcontrib>Zaric, Bozidarka</creatorcontrib><title>Lsm proteins bind and stabilize RNAs containing 5′ poly(A) tracts</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><description>Many orthopoxvirus messenger RNAs have an unusual nontemplated poly(A) tract of 5 to 40 residues at the 5' end. The precise function of this feature is unknown. Here we show that 5' poly(A) tracts are able to repress RNA decay by inhibiting 3'-to-5' exonucleases as well as decapping of RNA substrates. UV cross-linking analysis demonstrated that the Lsm complex associates with the 5' poly(A) tract. Furthermore, recombinant Lsm1-7 complex specifically binds 5' poly(A) tracts 10 to 21 nucleotides in length, consistent with the length of 5' poly(A) required for stabilization. Knockdown of Lsm1 abrogates RNA stabilization by the 5' poly(A) tract. We propose that the Lsm complex simultaneously binds the 3' and 5' ends of these unusual messenger RNAs and thereby prevents 3'-to-5' decay. The implications of this phenomenon for cellular mRNA decay are discussed.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding proteins</subject><subject>Cell Line</subject><subject>Cricetinae</subject><subject>Crosslinking</subject><subject>Decay</subject><subject>DNA Primers</subject><subject>Genetic aspects</subject><subject>Genetic recombination</subject><subject>Genetic translation</subject><subject>LSm proteins</subject><subject>Membrane Proteins - metabolism</subject><subject>Messenger RNA</subject><subject>Molecular biology</subject><subject>mRNA turnover</subject><subject>Nucleotides</subject><subject>Orthopoxvirus</subject><subject>Physiological aspects</subject><subject>Poly A - metabolism</subject><subject>Polyadenine</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Recombinant Proteins - metabolism</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA - chemistry</subject><subject>RNA - 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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>Bergman, Naomi</au><au>Anderson, John R</au><au>Schneider, Robert J</au><au>Kambach, Christian</au><au>Moraes, Karen C M</au><au>Wilusz, Carol J</au><au>Wilusz, Jeffrey</au><au>Zaric, Bozidarka</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lsm proteins bind and stabilize RNAs containing 5′ poly(A) tracts</atitle><jtitle>Nature structural & molecular biology</jtitle><addtitle>Nat Struct Mol Biol</addtitle><date>2007-09-01</date><risdate>2007</risdate><volume>14</volume><issue>9</issue><spage>824</spage><epage>831</epage><pages>824-831</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Many orthopoxvirus messenger RNAs have an unusual nontemplated poly(A) tract of 5 to 40 residues at the 5' end. 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| subjects | Animals Base Sequence Binding proteins Cell Line Cricetinae Crosslinking Decay DNA Primers Genetic aspects Genetic recombination Genetic translation LSm proteins Membrane Proteins - metabolism Messenger RNA Molecular biology mRNA turnover Nucleotides Orthopoxvirus Physiological aspects Poly A - metabolism Polyadenine Protein Binding Proteins Recombinant Proteins - metabolism Ribonucleic acid RNA RNA - chemistry RNA - metabolism Stabilization Substrates Ultraviolet Rays Viruses |
| title | Lsm proteins bind and stabilize RNAs containing 5′ poly(A) tracts |
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