Structure of Pumilio Reveals Similarity between RNA and Peptide Binding Motifs
Translation regulation plays an essential role in the differentiation and development of animal cells. One well-studied case is the control of hunchback mRNA during early Drosophila embryogenesis by the trans-acting factors Pumilio, Nanos, and Brain Tumor. We report here a crystal structure of the c...
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| Veröffentlicht in: | Cell 2001-04, Vol.105 (2), p.281-289 |
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| creator | Edwards, Thomas A Pyle, Scott E Wharton, Robin P Aggarwal, Aneel K |
| description | Translation regulation plays an essential role in the differentiation and development of animal cells. One well-studied case is the control of
hunchback mRNA during early
Drosophila embryogenesis by the trans-acting factors Pumilio, Nanos, and Brain Tumor. We report here a crystal structure of the critical region of Pumilio, the Puf domain, that organizes a multivalent repression complex on the 3′ untranslated region of
hunchback mRNA. The structure reveals an extended, rainbow shaped molecule, with tandem helical repeats that bear unexpected resemblance to the armadillo repeats in β-catenin and the HEAT repeats in protein phosphatase 2A. Based on the structure and genetic experiments, we identify putative interaction surfaces for
hunchback mRNA and the cofactors Nanos and Brain Tumor. This analysis suggests that similar features in helical repeat proteins are used to bind extended peptides and RNA. |
| doi_str_mv | 10.1016/S0092-8674(01)00318-X |
| format | Article |
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hunchback mRNA during early
Drosophila embryogenesis by the trans-acting factors Pumilio, Nanos, and Brain Tumor. We report here a crystal structure of the critical region of Pumilio, the Puf domain, that organizes a multivalent repression complex on the 3′ untranslated region of
hunchback mRNA. The structure reveals an extended, rainbow shaped molecule, with tandem helical repeats that bear unexpected resemblance to the armadillo repeats in β-catenin and the HEAT repeats in protein phosphatase 2A. Based on the structure and genetic experiments, we identify putative interaction surfaces for
hunchback mRNA and the cofactors Nanos and Brain Tumor. This analysis suggests that similar features in helical repeat proteins are used to bind extended peptides and RNA.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(01)00318-X</identifier><identifier>PMID: 11336677</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Animals ; BASIC BIOLOGICAL SCIENCES ; Brain Tumor protein ; Crystallography, X-Ray ; DNA-Binding Proteins ; Drosophila ; Drosophila melanogaster - chemistry ; Drosophila melanogaster - physiology ; Drosophila Proteins ; hunchback (hb) gene ; Insect Proteins - chemistry ; Insect Proteins - genetics ; Insect Proteins - metabolism ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Nanos protein ; NATIONAL SYNCHROTRON LIGHT SOURCE ; NSLS ; PEPTIDES ; Point Mutation ; Protein Structure, Tertiary ; Pumilio protein ; RNA ; RNA - chemistry ; RNA - metabolism ; RNA-Binding Proteins</subject><ispartof>Cell, 2001-04, Vol.105 (2), p.281-289</ispartof><rights>2001 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c531t-dfc836303a372369a0ded88c1fe7b9eebc11ad43eba1f274bd4ac4b12dbbadd83</citedby><cites>FETCH-LOGICAL-c531t-dfc836303a372369a0ded88c1fe7b9eebc11ad43eba1f274bd4ac4b12dbbadd83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0092-8674(01)00318-X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11336677$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/796526$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Edwards, Thomas A</creatorcontrib><creatorcontrib>Pyle, Scott E</creatorcontrib><creatorcontrib>Wharton, Robin P</creatorcontrib><creatorcontrib>Aggarwal, Aneel K</creatorcontrib><creatorcontrib>Brookhaven National Lab., Upton, NY (US)</creatorcontrib><creatorcontrib>National Synchrotron Light Source (US)</creatorcontrib><title>Structure of Pumilio Reveals Similarity between RNA and Peptide Binding Motifs</title><title>Cell</title><addtitle>Cell</addtitle><description>Translation regulation plays an essential role in the differentiation and development of animal cells. One well-studied case is the control of
hunchback mRNA during early
Drosophila embryogenesis by the trans-acting factors Pumilio, Nanos, and Brain Tumor. We report here a crystal structure of the critical region of Pumilio, the Puf domain, that organizes a multivalent repression complex on the 3′ untranslated region of
hunchback mRNA. The structure reveals an extended, rainbow shaped molecule, with tandem helical repeats that bear unexpected resemblance to the armadillo repeats in β-catenin and the HEAT repeats in protein phosphatase 2A. Based on the structure and genetic experiments, we identify putative interaction surfaces for
hunchback mRNA and the cofactors Nanos and Brain Tumor. This analysis suggests that similar features in helical repeat proteins are used to bind extended peptides and RNA.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Brain Tumor protein</subject><subject>Crystallography, X-Ray</subject><subject>DNA-Binding Proteins</subject><subject>Drosophila</subject><subject>Drosophila melanogaster - chemistry</subject><subject>Drosophila melanogaster - physiology</subject><subject>Drosophila Proteins</subject><subject>hunchback (hb) gene</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - metabolism</subject><subject>Macromolecular Substances</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nanos protein</subject><subject>NATIONAL SYNCHROTRON LIGHT SOURCE</subject><subject>NSLS</subject><subject>PEPTIDES</subject><subject>Point Mutation</subject><subject>Protein Structure, Tertiary</subject><subject>Pumilio protein</subject><subject>RNA</subject><subject>RNA - chemistry</subject><subject>RNA - metabolism</subject><subject>RNA-Binding Proteins</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV9PFDEUxRujkRX9CJr6QvRhsHc603aeDBBQE0TCQsJb0z93oGR3urYdDN_eWXYDjzzd3OR37sk9h5CPwPaBgfg2Z6yrKyVk84XBV8Y4qOr6FZkB62TVgKxfk9kTskPe5XzHGFNt274lOwCcCyHljJzNSxpdGRPS2NPzcRkWIdILvEezyHQept2kUB6oxfIPcaAXZwfUDJ6e46oEj_QwDD4MN_R3LKHP78mbfhLih-3cJVcnx5dHP6vTPz9-HR2cVq7lUCrfO8UFZ9xwWXPRGebRK-WgR2k7ROsAjG84WgN9LRvrG-MaC7W31niv-C75vLkbcwk6u1DQ3bo4DOiKlp1oazExextmleLfEXPRy5AdLhZmwDhmLZmCRnT8RRCkEg1XMIHtBnQp5pyw16sUliY9aGB63Yp-bEWvI9cM9GMr-nrSfdoajHaJ_lm1rWECvm8AnDK7D5jWL-Hg0Ie0_sjH8ILFf-gQnO0</recordid><startdate>20010420</startdate><enddate>20010420</enddate><creator>Edwards, Thomas A</creator><creator>Pyle, Scott E</creator><creator>Wharton, Robin P</creator><creator>Aggarwal, Aneel K</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7TM</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20010420</creationdate><title>Structure of Pumilio Reveals Similarity between RNA and Peptide Binding Motifs</title><author>Edwards, Thomas A ; Pyle, Scott E ; Wharton, Robin P ; Aggarwal, Aneel K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c531t-dfc836303a372369a0ded88c1fe7b9eebc11ad43eba1f274bd4ac4b12dbbadd83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Brain Tumor protein</topic><topic>Crystallography, X-Ray</topic><topic>DNA-Binding Proteins</topic><topic>Drosophila</topic><topic>Drosophila melanogaster - chemistry</topic><topic>Drosophila melanogaster - physiology</topic><topic>Drosophila Proteins</topic><topic>hunchback (hb) gene</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Macromolecular Substances</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nanos protein</topic><topic>NATIONAL SYNCHROTRON LIGHT SOURCE</topic><topic>NSLS</topic><topic>PEPTIDES</topic><topic>Point Mutation</topic><topic>Protein Structure, Tertiary</topic><topic>Pumilio protein</topic><topic>RNA</topic><topic>RNA - chemistry</topic><topic>RNA - metabolism</topic><topic>RNA-Binding Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Edwards, Thomas A</creatorcontrib><creatorcontrib>Pyle, Scott E</creatorcontrib><creatorcontrib>Wharton, Robin P</creatorcontrib><creatorcontrib>Aggarwal, Aneel K</creatorcontrib><creatorcontrib>Brookhaven National Lab., Upton, NY (US)</creatorcontrib><creatorcontrib>National Synchrotron Light Source (US)</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Edwards, Thomas A</au><au>Pyle, Scott E</au><au>Wharton, Robin P</au><au>Aggarwal, Aneel K</au><aucorp>Brookhaven National Lab., Upton, NY (US)</aucorp><aucorp>National Synchrotron Light Source (US)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of Pumilio Reveals Similarity between RNA and Peptide Binding Motifs</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2001-04-20</date><risdate>2001</risdate><volume>105</volume><issue>2</issue><spage>281</spage><epage>289</epage><pages>281-289</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Translation regulation plays an essential role in the differentiation and development of animal cells. One well-studied case is the control of
hunchback mRNA during early
Drosophila embryogenesis by the trans-acting factors Pumilio, Nanos, and Brain Tumor. We report here a crystal structure of the critical region of Pumilio, the Puf domain, that organizes a multivalent repression complex on the 3′ untranslated region of
hunchback mRNA. The structure reveals an extended, rainbow shaped molecule, with tandem helical repeats that bear unexpected resemblance to the armadillo repeats in β-catenin and the HEAT repeats in protein phosphatase 2A. Based on the structure and genetic experiments, we identify putative interaction surfaces for
hunchback mRNA and the cofactors Nanos and Brain Tumor. This analysis suggests that similar features in helical repeat proteins are used to bind extended peptides and RNA.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11336677</pmid><doi>10.1016/S0092-8674(01)00318-X</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals |
| subjects | Amino Acid Motifs Amino Acid Sequence Animals BASIC BIOLOGICAL SCIENCES Brain Tumor protein Crystallography, X-Ray DNA-Binding Proteins Drosophila Drosophila melanogaster - chemistry Drosophila melanogaster - physiology Drosophila Proteins hunchback (hb) gene Insect Proteins - chemistry Insect Proteins - genetics Insect Proteins - metabolism Macromolecular Substances Models, Molecular Molecular Sequence Data Nanos protein NATIONAL SYNCHROTRON LIGHT SOURCE NSLS PEPTIDES Point Mutation Protein Structure, Tertiary Pumilio protein RNA RNA - chemistry RNA - metabolism RNA-Binding Proteins |
| title | Structure of Pumilio Reveals Similarity between RNA and Peptide Binding Motifs |
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