Active Disruption of an RNA-Protein Interaction by a DExH/D RNA Helicase
All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are comp...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2001-01, Vol.291 (5501), p.121-125 |
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| creator | Jankowsky, Eckhard Gross, Christian H. Shuman, Stewart Pyle, Anna Marie |
| description | All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are complexed with proteins. It has therefore been speculated that DExH/D proteins may also affect RNA-protein interactions. We demonstrate that the DExH protein NPH-II from vaccinia virus can displace the protein U1A from RNA in an active adenosine triphosphate-dependent fashion. NPH-II increases the rate of U1A dissociation by more than three orders of magnitude while retaining helicase processivity. This indicates that DExH/D proteins can effectively catalyze protein displacement from RNA and thereby participate in the structural reorganization of ribonucleoprotein assemblies. |
| doi_str_mv | 10.1126/science.291.5501.121 |
| format | Article |
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Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are complexed with proteins. It has therefore been speculated that DExH/D proteins may also affect RNA-protein interactions. We demonstrate that the DExH protein NPH-II from vaccinia virus can displace the protein U1A from RNA in an active adenosine triphosphate-dependent fashion. NPH-II increases the rate of U1A dissociation by more than three orders of magnitude while retaining helicase processivity. This indicates that DExH/D proteins can effectively catalyze protein displacement from RNA and thereby participate in the structural reorganization of ribonucleoprotein assemblies.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.291.5501.121</identifier><identifier>PMID: 11141562</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>3' Untranslated Regions - metabolism ; Acid Anhydride Hydrolases - chemistry ; Acid Anhydride Hydrolases - metabolism ; Adenosine Triphosphate - metabolism ; Analysis ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Binding Sites ; Biochemistry ; Biodiversity conservation ; Biological and medical sciences ; DExH/D protein ; Dimers ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Land clearing ; Literary Devices ; Metabolism ; Models, Molecular ; Molecular Sequence Data ; NPH-II protein ; Nucleic Acid Conformation ; Nucleic acids ; Nucleoside-Triphosphatase ; Nucleotides ; Protected areas ; Protein Binding ; Protein Conformation ; Proteins ; Ribonucleic acid ; Ribonucleoprotein, U1 Small Nuclear - metabolism ; RNA ; RNA - chemistry ; RNA - metabolism ; RNA Helicases - chemistry ; RNA Helicases - metabolism ; Rna, ribonucleoproteins ; RNA-Binding Proteins ; Room temperature ; U1A protein ; Untranslated regions ; Vaccinia virus ; Viruses</subject><ispartof>Science (American Association for the Advancement of Science), 2001-01, Vol.291 (5501), p.121-125</ispartof><rights>Copyright 2001 American Association for the Advancement of Science</rights><rights>2001 INIST-CNRS</rights><rights>COPYRIGHT 2001 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2001 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Jan 5, 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c716t-73cd2fb75c3fcaa613f2eedb340a25eae24a986e50135332c257ecadff387d963</citedby><cites>FETCH-LOGICAL-c716t-73cd2fb75c3fcaa613f2eedb340a25eae24a986e50135332c257ecadff387d963</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3082188$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3082188$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>315,782,786,805,2886,2887,27931,27932,58024,58257</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=928645$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11141562$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jankowsky, Eckhard</creatorcontrib><creatorcontrib>Gross, Christian H.</creatorcontrib><creatorcontrib>Shuman, Stewart</creatorcontrib><creatorcontrib>Pyle, Anna Marie</creatorcontrib><title>Active Disruption of an RNA-Protein Interaction by a DExH/D RNA Helicase</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. 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| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2001-01, Vol.291 (5501), p.121-125 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743069640 |
| source | MEDLINE; Science Magazine; JSTOR Archive Collection A-Z Listing |
| subjects | 3' Untranslated Regions - metabolism Acid Anhydride Hydrolases - chemistry Acid Anhydride Hydrolases - metabolism Adenosine Triphosphate - metabolism Analysis Analytical, structural and metabolic biochemistry Base Sequence Binding Sites Biochemistry Biodiversity conservation Biological and medical sciences DExH/D protein Dimers Fundamental and applied biological sciences. Psychology Kinetics Land clearing Literary Devices Metabolism Models, Molecular Molecular Sequence Data NPH-II protein Nucleic Acid Conformation Nucleic acids Nucleoside-Triphosphatase Nucleotides Protected areas Protein Binding Protein Conformation Proteins Ribonucleic acid Ribonucleoprotein, U1 Small Nuclear - metabolism RNA RNA - chemistry RNA - metabolism RNA Helicases - chemistry RNA Helicases - metabolism Rna, ribonucleoproteins RNA-Binding Proteins Room temperature U1A protein Untranslated regions Vaccinia virus Viruses |
| title | Active Disruption of an RNA-Protein Interaction by a DExH/D RNA Helicase |
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