Interaction of the U3-55k protein with U3 snoRNA is mediated by the box B/C motif of U3 and the WD repeats of U3-55k
U3 small nucleolar RNA (snoRNA) is a member of the Box C/D family of snoRNAs which functions in ribosomal RNA processing. U3-55k is a protein that has been found to interact with U3 but not other members of the Box C/D snoRNA family. We have found that interaction of the U3-55k protein with U3 RNA i...
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Veröffentlicht in: | Nucleic acids research 2000-09, Vol.28 (18), p.3462-3471 |
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creator | Lukowiak, A A Granneman, S Mattox, S A Speckmann, W A Jones, K Pluk, H Venrooij, W J Terns, R M Terns, M P |
description | U3 small nucleolar RNA (snoRNA) is a member of the Box C/D family of snoRNAs which functions in ribosomal RNA processing. U3-55k is a protein that has been found to interact with U3 but not other members of the Box C/D snoRNA family. We have found that interaction of the U3-55k protein with U3 RNA in vivo is mediated by the conserved Box B/C motif which is unique to U3 snoRNA. Mutation of Box B and Box C, but not of other conserved sequence elements, disrupted interaction of U3-55k with U3 RNA. Furthermore, a fragment of U3 containing only these two conserved elements was bound by U3-55k in vivo. RNA binding assays performed in vitro indicate that Box C may be the primary determinant of the interaction. We have cloned the cDNA encoding the Xenopus laevis U3-55k protein and find strong homology to the human sequence, including six WD repeats. Deletion of WD repeats or sequences near the C-terminus of U3-55k resulted in loss of association with U3 RNA and also loss of localization of U3-55k to the nucleolus, suggesting that protein-protein interactions contribute to the localization and RNA binding of U3-55k in vivo. |
doi_str_mv | 10.1093/nar/28.18.3462 |
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U3-55k is a protein that has been found to interact with U3 but not other members of the Box C/D snoRNA family. We have found that interaction of the U3-55k protein with U3 RNA in vivo is mediated by the conserved Box B/C motif which is unique to U3 snoRNA. Mutation of Box B and Box C, but not of other conserved sequence elements, disrupted interaction of U3-55k with U3 RNA. Furthermore, a fragment of U3 containing only these two conserved elements was bound by U3-55k in vivo. RNA binding assays performed in vitro indicate that Box C may be the primary determinant of the interaction. We have cloned the cDNA encoding the Xenopus laevis U3-55k protein and find strong homology to the human sequence, including six WD repeats. Deletion of WD repeats or sequences near the C-terminus of U3-55k resulted in loss of association with U3 RNA and also loss of localization of U3-55k to the nucleolus, suggesting that protein-protein interactions contribute to the localization and RNA binding of U3-55k in vivo.</description><identifier>ISSN: 1362-4962</identifier><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/28.18.3462</identifier><identifier>PMID: 10982864</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>England: Oxford Publishing Limited (England)</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cloning, Molecular ; Humans ; Molecular Sequence Data ; Protein Binding ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Repetitive Sequences, Nucleic Acid ; Ribonucleoproteins, Small Nucleolar - chemistry ; Ribonucleoproteins, Small Nucleolar - metabolism ; RNA, Small Nucleolar - chemistry ; RNA, Small Nucleolar - metabolism ; Sequence Homology, Amino Acid ; snoRNA U3 ; U3-55K protein ; Xenopus laevis</subject><ispartof>Nucleic acids research, 2000-09, Vol.28 (18), p.3462-3471</ispartof><rights>Copyright Oxford University Press(England) Sep 15, 2000</rights><rights>Copyright © 2000 Oxford University Press 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-131ae3769a4f11e210c38a9f4f59c97896168197aaa118e7cd4f21fd71df88e33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC110750/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC110750/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10982864$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lukowiak, A A</creatorcontrib><creatorcontrib>Granneman, S</creatorcontrib><creatorcontrib>Mattox, S A</creatorcontrib><creatorcontrib>Speckmann, W A</creatorcontrib><creatorcontrib>Jones, K</creatorcontrib><creatorcontrib>Pluk, H</creatorcontrib><creatorcontrib>Venrooij, W J</creatorcontrib><creatorcontrib>Terns, R M</creatorcontrib><creatorcontrib>Terns, M P</creatorcontrib><title>Interaction of the U3-55k protein with U3 snoRNA is mediated by the box B/C motif of U3 and the WD repeats of U3-55k</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>U3 small nucleolar RNA (snoRNA) is a member of the Box C/D family of snoRNAs which functions in ribosomal RNA processing. U3-55k is a protein that has been found to interact with U3 but not other members of the Box C/D snoRNA family. We have found that interaction of the U3-55k protein with U3 RNA in vivo is mediated by the conserved Box B/C motif which is unique to U3 snoRNA. Mutation of Box B and Box C, but not of other conserved sequence elements, disrupted interaction of U3-55k with U3 RNA. Furthermore, a fragment of U3 containing only these two conserved elements was bound by U3-55k in vivo. RNA binding assays performed in vitro indicate that Box C may be the primary determinant of the interaction. We have cloned the cDNA encoding the Xenopus laevis U3-55k protein and find strong homology to the human sequence, including six WD repeats. Deletion of WD repeats or sequences near the C-terminus of U3-55k resulted in loss of association with U3 RNA and also loss of localization of U3-55k to the nucleolus, suggesting that protein-protein interactions contribute to the localization and RNA binding of U3-55k in vivo.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cloning, Molecular</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Protein Binding</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Repetitive Sequences, Nucleic Acid</subject><subject>Ribonucleoproteins, Small Nucleolar - chemistry</subject><subject>Ribonucleoproteins, Small Nucleolar - metabolism</subject><subject>RNA, Small Nucleolar - chemistry</subject><subject>RNA, Small Nucleolar - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>snoRNA U3</subject><subject>U3-55K protein</subject><subject>Xenopus laevis</subject><issn>1362-4962</issn><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1vVCEUxYmxsbW6dWmIC3dvhgs8PhYu6vjRJo0mxsYlYd4DhzoDIzBq_3t5naaZunEF4fzOyb0chF4AmQHRbB5tnlM1AzVjXNBH6ASYoB3Xgj4-uB-jp6VcEwIcev4EHTerokrwE1QvYnXZDjWkiJPHdeXwFev6_gfe5lRdiPh3qKv2hktMXz6d4VDwxo3BVjfi5c2tYZn-4LfzBd6kGvyU0mgbx1vt2zuc3dbZWvbCFP0MHXm7Lu753XmKrj68_7o47y4_f7xYnF12A-esdsDAOiaFttwDOApkYMpqz32vBy2VFiAUaGmtBVBODiP3FPwoYfRKOcZO0Zt97na3bDMPLtZs12abw8bmG5NsMA-VGFbme_plAIjsSfO_vvPn9HPnSjWbUAa3Xtvo0q4YSWnPJfk_CFJQ1ou-ga_-Aa_TLsf2CYYSIrjWZIJme2jIqZTs_P3EQMzUummtG6oMKDO13gwvD_c8wPc1s7-VF6WW</recordid><startdate>20000915</startdate><enddate>20000915</enddate><creator>Lukowiak, A A</creator><creator>Granneman, S</creator><creator>Mattox, S A</creator><creator>Speckmann, W A</creator><creator>Jones, K</creator><creator>Pluk, H</creator><creator>Venrooij, W J</creator><creator>Terns, R M</creator><creator>Terns, M P</creator><general>Oxford Publishing Limited (England)</general><general>Oxford University Press</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>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000915</creationdate><title>Interaction of the U3-55k protein with U3 snoRNA is mediated by the box B/C motif of U3 and the WD repeats of U3-55k</title><author>Lukowiak, A A ; Granneman, S ; Mattox, S A ; Speckmann, W A ; Jones, K ; Pluk, H ; Venrooij, W J ; Terns, R M ; Terns, M P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-131ae3769a4f11e210c38a9f4f59c97896168197aaa118e7cd4f21fd71df88e33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cloning, Molecular</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Protein Binding</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Repetitive Sequences, Nucleic Acid</topic><topic>Ribonucleoproteins, Small Nucleolar - chemistry</topic><topic>Ribonucleoproteins, Small Nucleolar - metabolism</topic><topic>RNA, Small Nucleolar - chemistry</topic><topic>RNA, Small Nucleolar - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>snoRNA U3</topic><topic>U3-55K protein</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lukowiak, A A</creatorcontrib><creatorcontrib>Granneman, S</creatorcontrib><creatorcontrib>Mattox, S A</creatorcontrib><creatorcontrib>Speckmann, W A</creatorcontrib><creatorcontrib>Jones, K</creatorcontrib><creatorcontrib>Pluk, H</creatorcontrib><creatorcontrib>Venrooij, W J</creatorcontrib><creatorcontrib>Terns, R M</creatorcontrib><creatorcontrib>Terns, M P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lukowiak, A A</au><au>Granneman, S</au><au>Mattox, S A</au><au>Speckmann, W A</au><au>Jones, K</au><au>Pluk, H</au><au>Venrooij, W J</au><au>Terns, R M</au><au>Terns, M P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of the U3-55k protein with U3 snoRNA is mediated by the box B/C motif of U3 and the WD repeats of U3-55k</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2000-09-15</date><risdate>2000</risdate><volume>28</volume><issue>18</issue><spage>3462</spage><epage>3471</epage><pages>3462-3471</pages><issn>1362-4962</issn><issn>0305-1048</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>U3 small nucleolar RNA (snoRNA) is a member of the Box C/D family of snoRNAs which functions in ribosomal RNA processing. U3-55k is a protein that has been found to interact with U3 but not other members of the Box C/D snoRNA family. We have found that interaction of the U3-55k protein with U3 RNA in vivo is mediated by the conserved Box B/C motif which is unique to U3 snoRNA. Mutation of Box B and Box C, but not of other conserved sequence elements, disrupted interaction of U3-55k with U3 RNA. Furthermore, a fragment of U3 containing only these two conserved elements was bound by U3-55k in vivo. RNA binding assays performed in vitro indicate that Box C may be the primary determinant of the interaction. We have cloned the cDNA encoding the Xenopus laevis U3-55k protein and find strong homology to the human sequence, including six WD repeats. Deletion of WD repeats or sequences near the C-terminus of U3-55k resulted in loss of association with U3 RNA and also loss of localization of U3-55k to the nucleolus, suggesting that protein-protein interactions contribute to the localization and RNA binding of U3-55k in vivo.</abstract><cop>England</cop><pub>Oxford Publishing Limited (England)</pub><pmid>10982864</pmid><doi>10.1093/nar/28.18.3462</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Motifs Amino Acid Sequence Animals Cloning, Molecular Humans Molecular Sequence Data Protein Binding Recombinant Proteins - genetics Recombinant Proteins - metabolism Repetitive Sequences, Nucleic Acid Ribonucleoproteins, Small Nucleolar - chemistry Ribonucleoproteins, Small Nucleolar - metabolism RNA, Small Nucleolar - chemistry RNA, Small Nucleolar - metabolism Sequence Homology, Amino Acid snoRNA U3 U3-55K protein Xenopus laevis |
title | Interaction of the U3-55k protein with U3 snoRNA is mediated by the box B/C motif of U3 and the WD repeats of U3-55k |
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