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The La RNA-binding Protein Interacts with the Vault RNA and Is a Vault-associated Protein
Vaults are highly conserved ubiquitous ribonucleoprotein particles with an undefined function. Three protein species (p240/TEP1, p193/VPARP, and p100/MVP) and a small RNA comprise the 13-MDa vault particle. The expression of the unique 100-kDa major vault protein is sufficient to form the basic vaul...
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| Published in: | The Journal of biological chemistry 2002-10, Vol.277 (43), p.41282-41286 |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
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| container_end_page | 41286 |
| container_issue | 43 |
| container_start_page | 41282 |
| container_title | The Journal of biological chemistry |
| container_volume | 277 |
| creator | Kickhoefer, Valerie A Poderycki, Michael J Chan, Edward K L Rome, Leonard H |
| description | Vaults are highly conserved ubiquitous ribonucleoprotein particles with an undefined function. Three protein species (p240/TEP1,
p193/VPARP, and p100/MVP) and a small RNA comprise the 13-MDa vault particle. The expression of the unique 100-kDa major vault
protein is sufficient to form the basic vault structure. Previously, we have shown that stable association of the vault RNA
with the vault particle is dependent on its interaction with the p240/TEP1 protein. To identify other proteins that interact
with the vault RNA, we used a UV-cross-linking assay. We find that a portion of the vault RNA is complexed with the La autoantigen
in a separate smaller ribonucleoprotein particle. La interacts with the vault RNA (both in vivo and in vitro ) presumably through binding to 3â²-uridylates. Moreover, we also demonstrate that the La autoantigen is the 50-kDa protein
that we have previously reported as a protein that co-purifies with vaults. |
| doi_str_mv | 10.1074/jbc.M206980200 |
| format | article |
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p193/VPARP, and p100/MVP) and a small RNA comprise the 13-MDa vault particle. The expression of the unique 100-kDa major vault
protein is sufficient to form the basic vault structure. Previously, we have shown that stable association of the vault RNA
with the vault particle is dependent on its interaction with the p240/TEP1 protein. To identify other proteins that interact
with the vault RNA, we used a UV-cross-linking assay. We find that a portion of the vault RNA is complexed with the La autoantigen
in a separate smaller ribonucleoprotein particle. La interacts with the vault RNA (both in vivo and in vitro ) presumably through binding to 3â²-uridylates. Moreover, we also demonstrate that the La autoantigen is the 50-kDa protein
that we have previously reported as a protein that co-purifies with vaults.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M206980200</identifier><identifier>PMID: 12196535</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Autoantigens ; HeLa Cells ; Humans ; Liver - metabolism ; Protein Binding ; Rats ; Ribonucleoproteins - isolation & purification ; Ribonucleoproteins - metabolism ; RNA - metabolism ; RNA-Binding Proteins - isolation & purification ; RNA-Binding Proteins - metabolism ; SS-B Antigen ; Vault Ribonucleoprotein Particles - isolation & purification ; Vault Ribonucleoprotein Particles - metabolism</subject><ispartof>The Journal of biological chemistry, 2002-10, Vol.277 (43), p.41282-41286</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-c36cdee97208539154043ba36f38971564afe7d4cb8c47d3b9655a8ecd3cb3a13</citedby><cites>FETCH-LOGICAL-c391t-c36cdee97208539154043ba36f38971564afe7d4cb8c47d3b9655a8ecd3cb3a13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12196535$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kickhoefer, Valerie A</creatorcontrib><creatorcontrib>Poderycki, Michael J</creatorcontrib><creatorcontrib>Chan, Edward K L</creatorcontrib><creatorcontrib>Rome, Leonard H</creatorcontrib><title>The La RNA-binding Protein Interacts with the Vault RNA and Is a Vault-associated Protein</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Vaults are highly conserved ubiquitous ribonucleoprotein particles with an undefined function. Three protein species (p240/TEP1,
p193/VPARP, and p100/MVP) and a small RNA comprise the 13-MDa vault particle. The expression of the unique 100-kDa major vault
protein is sufficient to form the basic vault structure. Previously, we have shown that stable association of the vault RNA
with the vault particle is dependent on its interaction with the p240/TEP1 protein. To identify other proteins that interact
with the vault RNA, we used a UV-cross-linking assay. We find that a portion of the vault RNA is complexed with the La autoantigen
in a separate smaller ribonucleoprotein particle. La interacts with the vault RNA (both in vivo and in vitro ) presumably through binding to 3â²-uridylates. Moreover, we also demonstrate that the La autoantigen is the 50-kDa protein
that we have previously reported as a protein that co-purifies with vaults.</description><subject>Animals</subject><subject>Autoantigens</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Liver - metabolism</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>Ribonucleoproteins - isolation & purification</subject><subject>Ribonucleoproteins - metabolism</subject><subject>RNA - metabolism</subject><subject>RNA-Binding Proteins - isolation & purification</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>SS-B Antigen</subject><subject>Vault Ribonucleoprotein Particles - isolation & purification</subject><subject>Vault Ribonucleoprotein Particles - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNqFkMtLAzEQh4MotlavHiUH8bY1z032WIqPQn0gVfQUstlsN2W7Wzcpxf_elFZ6dA4z8OObYfgAuMRoiJFgt4vcDJ8ISjOJCEJHoI-RpAnl-PMY9BEiOMkIlz1w5v0CxWIZPgU9THCWcsr74GtWWTjV8O15lOSuKVwzh69dG6xr4KQJttMmeLhxoYIhkh96XYctDHVTwImHehcl2vvWOB1s8bd-Dk5KXXt7sZ8D8H5_Nxs_JtOXh8l4NE0MzXCIPTWFtZkgSPKYcIYYzTVNSyozgXnKdGlFwUwuDRMFzePjXEtrCmpyqjEdgJvd3VXXfq-tD2rpvLF1rRvbrr0SJI1OmPgXxJIjQomM4HAHmq71vrOlWnVuqbsfhZHaWlfRujpYjwtX-8vrfGmLA77XHIHrHVC5ebVxnVW5a01ll4oIoRhVDBNJ6C9gfYeg</recordid><startdate>20021025</startdate><enddate>20021025</enddate><creator>Kickhoefer, Valerie A</creator><creator>Poderycki, Michael J</creator><creator>Chan, Edward K L</creator><creator>Rome, Leonard H</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20021025</creationdate><title>The La RNA-binding Protein Interacts with the Vault RNA and Is a Vault-associated Protein</title><author>Kickhoefer, Valerie A ; Poderycki, Michael J ; Chan, Edward K L ; Rome, Leonard H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-c36cdee97208539154043ba36f38971564afe7d4cb8c47d3b9655a8ecd3cb3a13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Autoantigens</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Liver - metabolism</topic><topic>Protein Binding</topic><topic>Rats</topic><topic>Ribonucleoproteins - isolation & purification</topic><topic>Ribonucleoproteins - metabolism</topic><topic>RNA - metabolism</topic><topic>RNA-Binding Proteins - isolation & purification</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>SS-B Antigen</topic><topic>Vault Ribonucleoprotein Particles - isolation & purification</topic><topic>Vault Ribonucleoprotein Particles - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kickhoefer, Valerie A</creatorcontrib><creatorcontrib>Poderycki, Michael J</creatorcontrib><creatorcontrib>Chan, Edward K L</creatorcontrib><creatorcontrib>Rome, Leonard H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kickhoefer, Valerie A</au><au>Poderycki, Michael J</au><au>Chan, Edward K L</au><au>Rome, Leonard H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The La RNA-binding Protein Interacts with the Vault RNA and Is a Vault-associated Protein</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2002-10-25</date><risdate>2002</risdate><volume>277</volume><issue>43</issue><spage>41282</spage><epage>41286</epage><pages>41282-41286</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Vaults are highly conserved ubiquitous ribonucleoprotein particles with an undefined function. Three protein species (p240/TEP1,
p193/VPARP, and p100/MVP) and a small RNA comprise the 13-MDa vault particle. The expression of the unique 100-kDa major vault
protein is sufficient to form the basic vault structure. Previously, we have shown that stable association of the vault RNA
with the vault particle is dependent on its interaction with the p240/TEP1 protein. To identify other proteins that interact
with the vault RNA, we used a UV-cross-linking assay. We find that a portion of the vault RNA is complexed with the La autoantigen
in a separate smaller ribonucleoprotein particle. La interacts with the vault RNA (both in vivo and in vitro ) presumably through binding to 3â²-uridylates. Moreover, we also demonstrate that the La autoantigen is the 50-kDa protein
that we have previously reported as a protein that co-purifies with vaults.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>12196535</pmid><doi>10.1074/jbc.M206980200</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2002-10, Vol.277 (43), p.41282-41286 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | ScienceDirect (Online service) |
| subjects | Animals Autoantigens HeLa Cells Humans Liver - metabolism Protein Binding Rats Ribonucleoproteins - isolation & purification Ribonucleoproteins - metabolism RNA - metabolism RNA-Binding Proteins - isolation & purification RNA-Binding Proteins - metabolism SS-B Antigen Vault Ribonucleoprotein Particles - isolation & purification Vault Ribonucleoprotein Particles - metabolism |
| title | The La RNA-binding Protein Interacts with the Vault RNA and Is a Vault-associated Protein |
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