Recognition and long-range interactions of a minimal nanos RNA localization signal element
Localization of nanos (nos) mRNA to the germ plasm at the posterior pole of the Drosophila embryo is essential to activate nos translation and thereby generate abdominal segments. nos RNA localization is mediated by a large cis-acting localization signal composed of multiple, partially redundant ele...
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| Veröffentlicht in: | Development (Cambridge) 2001-02, Vol.128 (3), p.427-435 |
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| creator | Bergsten, S E Huang, T Chatterjee, S Gavis, E R |
| description | Localization of nanos (nos) mRNA to the germ plasm at the posterior pole of the Drosophila embryo is essential to activate nos translation and thereby generate abdominal segments. nos RNA localization is mediated by a large cis-acting localization signal composed of multiple, partially redundant elements within the nos 3â² untranslated region. We identify a protein of approximately 75 kDa (p75) that interacts specifically with the nos +2â² localization signal element. We show that the function of this element can be delimited to a 41 nucleotide domain that is conserved between D. melanogaster and D. virilis, and confers near wild-type localization when present in three copies. Two small mutations within this domain eliminate both +2â² element localization function and p75 binding, consistent with a role for p75 in nos RNA localization. In the intact localization signal, the +2â² element collaborates with adjacent localization elements. We show that different +2â² element mutations not only abolish collaboration between the +2â² and adjacent +1 element but also produce long-range deleterious effects on localization signal function. Our results suggest that higher order structural interactions within the localization signal, which requires factors such as p75, are necessary for association of nos mRNA with the germ plasm. |
| doi_str_mv | 10.1242/dev.128.3.427 |
| format | Article |
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We identify a protein of approximately 75 kDa (p75) that interacts specifically with the nos +2â² localization signal element. We show that the function of this element can be delimited to a 41 nucleotide domain that is conserved between D. melanogaster and D. virilis, and confers near wild-type localization when present in three copies. Two small mutations within this domain eliminate both +2â² element localization function and p75 binding, consistent with a role for p75 in nos RNA localization. In the intact localization signal, the +2â² element collaborates with adjacent localization elements. We show that different +2â² element mutations not only abolish collaboration between the +2â² and adjacent +1 element but also produce long-range deleterious effects on localization signal function. Our results suggest that higher order structural interactions within the localization signal, which requires factors such as p75, are necessary for association of nos mRNA with the germ plasm.</description><identifier>ISSN: 0950-1991</identifier><identifier>EISSN: 1477-9129</identifier><identifier>DOI: 10.1242/dev.128.3.427</identifier><identifier>PMID: 11152641</identifier><language>eng</language><publisher>England: The Company of Biologists Limited</publisher><subject>3' Untranslated Regions - genetics ; Abdomen - embryology ; Animals ; Animals, Genetically Modified ; Base Sequence ; Biological Transport ; Body Patterning ; Conserved Sequence ; Cytoplasm - metabolism ; Drosophila ; Drosophila - cytology ; Drosophila - embryology ; Drosophila - genetics ; Drosophila Proteins ; Female ; Gene Expression Regulation, Developmental ; In Situ Hybridization ; Insect Hormones - genetics ; Insect Proteins - genetics ; Molecular Weight ; Mutation - genetics ; nanos (nos) gene ; p75 protein ; Protein Binding ; Protein Biosynthesis ; Protein Structure, Tertiary ; Regulatory Sequences, Nucleic Acid - genetics ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - metabolism</subject><ispartof>Development (Cambridge), 2001-02, Vol.128 (3), p.427-435</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-b007b78991132187cd417b8dd799274ed3784ff52da648ea9dfb4b46406085c3</citedby><cites>FETCH-LOGICAL-c357t-b007b78991132187cd417b8dd799274ed3784ff52da648ea9dfb4b46406085c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3678,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11152641$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bergsten, S E</creatorcontrib><creatorcontrib>Huang, T</creatorcontrib><creatorcontrib>Chatterjee, S</creatorcontrib><creatorcontrib>Gavis, E R</creatorcontrib><title>Recognition and long-range interactions of a minimal nanos RNA localization signal element</title><title>Development (Cambridge)</title><addtitle>Development</addtitle><description>Localization of nanos (nos) mRNA to the germ plasm at the posterior pole of the Drosophila embryo is essential to activate nos translation and thereby generate abdominal segments. nos RNA localization is mediated by a large cis-acting localization signal composed of multiple, partially redundant elements within the nos 3â² untranslated region. We identify a protein of approximately 75 kDa (p75) that interacts specifically with the nos +2â² localization signal element. We show that the function of this element can be delimited to a 41 nucleotide domain that is conserved between D. melanogaster and D. virilis, and confers near wild-type localization when present in three copies. Two small mutations within this domain eliminate both +2â² element localization function and p75 binding, consistent with a role for p75 in nos RNA localization. In the intact localization signal, the +2â² element collaborates with adjacent localization elements. We show that different +2â² element mutations not only abolish collaboration between the +2â² and adjacent +1 element but also produce long-range deleterious effects on localization signal function. Our results suggest that higher order structural interactions within the localization signal, which requires factors such as p75, are necessary for association of nos mRNA with the germ plasm.</description><subject>3' Untranslated Regions - genetics</subject><subject>Abdomen - embryology</subject><subject>Animals</subject><subject>Animals, Genetically Modified</subject><subject>Base Sequence</subject><subject>Biological Transport</subject><subject>Body Patterning</subject><subject>Conserved Sequence</subject><subject>Cytoplasm - metabolism</subject><subject>Drosophila</subject><subject>Drosophila - cytology</subject><subject>Drosophila - embryology</subject><subject>Drosophila - genetics</subject><subject>Drosophila Proteins</subject><subject>Female</subject><subject>Gene Expression Regulation, Developmental</subject><subject>In Situ Hybridization</subject><subject>Insect Hormones - genetics</subject><subject>Insect Proteins - genetics</subject><subject>Molecular Weight</subject><subject>Mutation - genetics</subject><subject>nanos (nos) gene</subject><subject>p75 protein</subject><subject>Protein Binding</subject><subject>Protein Biosynthesis</subject><subject>Protein Structure, Tertiary</subject><subject>Regulatory Sequences, Nucleic Acid - genetics</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - metabolism</subject><issn>0950-1991</issn><issn>1477-9129</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkL1PwzAQxS0EglIYWVEmJlL8lTgeEeJLQiBVnVgsJ74EI8cucQqCvx6XVoKN6Z50v3t39xA6IXhGKKcXBt6TqGZsxqnYQRPChcgloXIXTbAscE6kJAfoMMZXjDErhdhHB4SQgpacTNDzHJrQeTva4DPtTeaC7_JB-w4y60cYdLNuxSy0mc56622vXea1DzGbP14mvNHOfumf-Wg7n7rgoAc_HqG9VrsIx9s6RYub68XVXf7wdHt_dfmQN6wQY15jLGpRpSsJo6QSjeFE1JUxQkoqOBgmKt62BTW65BVoadqa17zkuMRV0bApOtvYLofwtoI4qt7GBpzTHsIqKoELyQil_4Ik7ZGMiwTmG7AZQowDtGo5pLeHT0WwWoeuUuhJVIqpFHriT7fGq7oH80tvU07A-QZ4sd3Lhx1A1Ta40Nk4xrUXuLD84_cNICKM6g</recordid><startdate>20010201</startdate><enddate>20010201</enddate><creator>Bergsten, S E</creator><creator>Huang, T</creator><creator>Chatterjee, S</creator><creator>Gavis, E R</creator><general>The Company of Biologists Limited</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>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20010201</creationdate><title>Recognition and long-range interactions of a minimal nanos RNA localization signal element</title><author>Bergsten, S E ; Huang, T ; Chatterjee, S ; Gavis, E R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-b007b78991132187cd417b8dd799274ed3784ff52da648ea9dfb4b46406085c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>3' Untranslated Regions - genetics</topic><topic>Abdomen - embryology</topic><topic>Animals</topic><topic>Animals, Genetically Modified</topic><topic>Base Sequence</topic><topic>Biological Transport</topic><topic>Body Patterning</topic><topic>Conserved Sequence</topic><topic>Cytoplasm - metabolism</topic><topic>Drosophila</topic><topic>Drosophila - cytology</topic><topic>Drosophila - embryology</topic><topic>Drosophila - genetics</topic><topic>Drosophila Proteins</topic><topic>Female</topic><topic>Gene Expression Regulation, Developmental</topic><topic>In Situ Hybridization</topic><topic>Insect Hormones - genetics</topic><topic>Insect Proteins - genetics</topic><topic>Molecular Weight</topic><topic>Mutation - genetics</topic><topic>nanos (nos) gene</topic><topic>p75 protein</topic><topic>Protein Binding</topic><topic>Protein Biosynthesis</topic><topic>Protein Structure, Tertiary</topic><topic>Regulatory Sequences, Nucleic Acid - genetics</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bergsten, S E</creatorcontrib><creatorcontrib>Huang, T</creatorcontrib><creatorcontrib>Chatterjee, S</creatorcontrib><creatorcontrib>Gavis, E R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Development (Cambridge)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bergsten, S E</au><au>Huang, T</au><au>Chatterjee, S</au><au>Gavis, E R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recognition and long-range interactions of a minimal nanos RNA localization signal element</atitle><jtitle>Development (Cambridge)</jtitle><addtitle>Development</addtitle><date>2001-02-01</date><risdate>2001</risdate><volume>128</volume><issue>3</issue><spage>427</spage><epage>435</epage><pages>427-435</pages><issn>0950-1991</issn><eissn>1477-9129</eissn><abstract>Localization of nanos (nos) mRNA to the germ plasm at the posterior pole of the Drosophila embryo is essential to activate nos translation and thereby generate abdominal segments. nos RNA localization is mediated by a large cis-acting localization signal composed of multiple, partially redundant elements within the nos 3â² untranslated region. We identify a protein of approximately 75 kDa (p75) that interacts specifically with the nos +2â² localization signal element. We show that the function of this element can be delimited to a 41 nucleotide domain that is conserved between D. melanogaster and D. virilis, and confers near wild-type localization when present in three copies. Two small mutations within this domain eliminate both +2â² element localization function and p75 binding, consistent with a role for p75 in nos RNA localization. In the intact localization signal, the +2â² element collaborates with adjacent localization elements. We show that different +2â² element mutations not only abolish collaboration between the +2â² and adjacent +1 element but also produce long-range deleterious effects on localization signal function. 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| ispartof | Development (Cambridge), 2001-02, Vol.128 (3), p.427-435 |
| issn | 0950-1991 1477-9129 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection; Company of Biologists |
| subjects | 3' Untranslated Regions - genetics Abdomen - embryology Animals Animals, Genetically Modified Base Sequence Biological Transport Body Patterning Conserved Sequence Cytoplasm - metabolism Drosophila Drosophila - cytology Drosophila - embryology Drosophila - genetics Drosophila Proteins Female Gene Expression Regulation, Developmental In Situ Hybridization Insect Hormones - genetics Insect Proteins - genetics Molecular Weight Mutation - genetics nanos (nos) gene p75 protein Protein Binding Protein Biosynthesis Protein Structure, Tertiary Regulatory Sequences, Nucleic Acid - genetics RNA, Messenger - genetics RNA, Messenger - metabolism RNA-Binding Proteins - chemistry RNA-Binding Proteins - metabolism |
| title | Recognition and long-range interactions of a minimal nanos RNA localization signal element |
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