Loading…
The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction
Src homology 3 (SH3) domains are small non‐catalytic protein modules capable of mediating protein–protein interactions by binding to proline‐X‐X‐proline (P‐X‐X‐P) motifs. Here we demonstrate that the SH3 domain of the integral peroxisomal membrane protein Pex13p is able to bind two proteins, one of...
Saved in:
| Published in: | The EMBO journal 2000-12, Vol.19 (23), p.6382-6391 |
|---|---|
| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c6361-d06e002fe4b5c9c2533afa93494899bd6abd7758254459b9c64c29f4aa2c9d3 |
|---|---|
| cites | |
| container_end_page | 6391 |
| container_issue | 23 |
| container_start_page | 6382 |
| container_title | The EMBO journal |
| container_volume | 19 |
| creator | Barnett, Phil Bottger, Gina Klein, André T.J. Tabak, Henk F. Distel, Ben |
| description | Src homology 3 (SH3) domains are small non‐catalytic protein modules capable of mediating protein–protein interactions by binding to proline‐X‐X‐proline (P‐X‐X‐P) motifs. Here we demonstrate that the SH3 domain of the integral peroxisomal membrane protein Pex13p is able to bind two proteins, one of which, Pex5p, represents a novel non‐P‐X‐X‐P ligand. Using alanine scanning, two‐hybrid and
in vitro
interaction analysis, we show that an α‐helical element in Pex5p is necessary and sufficient for SH3 interaction. Sup pressor analysis using Pex5p mutants located in this α‐helical element allowed the identification of a unique site of interaction for Pex5p on the Pex13p‐SH3 domain that is distinct from the classical P‐X‐X‐P binding pocket. On the basis of a structural model of the Pex13p‐SH3 domain we show that this interaction probably takes place between the RT‐ and distal loops. Thus, the Pex13p‐SH3–Pex5p interaction establishes a novel mode of SH3 interaction. |
| doi_str_mv | 10.1093/emboj/19.23.6382 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_305852</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>374524891</sourcerecordid><originalsourceid>FETCH-LOGICAL-c6361-d06e002fe4b5c9c2533afa93494899bd6abd7758254459b9c64c29f4aa2c9d3</originalsourceid><addsrcrecordid>eNqFkM1vEzEQxS1ERUPLnQvI4r6pP3fXBw40Ki00LaBWytHy7s42Dlk72Js2_e9x2CgtB8TJkuf93rx5CL2lZEyJ4ifQVX5xQtWY8XHOS_YCjajIScZIIV-iEWE5zQQt1SF6HeOCECLLgr5Ch5RSQiWlI3R1Owe8guA3NvrOLHGXPINx6TP4HqzD32FD-QrHuX-I2GDn7yGpfAPYt_jmgmPregim7q13x-igNcsIb3bvEbr5fHY7ucim386_TD5NszrnKVJDciCEtSAqWauaSc5NaxQXSpRKVU1uqqYoZMmkEFJVqs5FzVQrjGG1avgR-ji4rtZVB00Nrg9mqVfBdiY8am-s_nvi7Fzf-XvN0_2SJf7Djg_-1xpirxd-HVwKrKmSaalkZRKRQVQHH2OAdu9Pid6Wr_-UnwjNuN6Wn5D3z3M9Abu2k0ANgge7hMf_Guqzq9OvhUy9yC1LBzYmzN1BeBb634HeDYwz_TrAfuGTZzbMbexhsx-b8FPnBS-knl2f62J6OZOTWal_8N8QhbxK</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>195254528</pqid></control><display><type>article</type><title>The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction</title><source>PubMed Central (PMC)</source><creator>Barnett, Phil ; Bottger, Gina ; Klein, André T.J. ; Tabak, Henk F. ; Distel, Ben</creator><creatorcontrib>Barnett, Phil ; Bottger, Gina ; Klein, André T.J. ; Tabak, Henk F. ; Distel, Ben</creatorcontrib><description>Src homology 3 (SH3) domains are small non‐catalytic protein modules capable of mediating protein–protein interactions by binding to proline‐X‐X‐proline (P‐X‐X‐P) motifs. Here we demonstrate that the SH3 domain of the integral peroxisomal membrane protein Pex13p is able to bind two proteins, one of which, Pex5p, represents a novel non‐P‐X‐X‐P ligand. Using alanine scanning, two‐hybrid and
in vitro
interaction analysis, we show that an α‐helical element in Pex5p is necessary and sufficient for SH3 interaction. Sup pressor analysis using Pex5p mutants located in this α‐helical element allowed the identification of a unique site of interaction for Pex5p on the Pex13p‐SH3 domain that is distinct from the classical P‐X‐X‐P binding pocket. On the basis of a structural model of the Pex13p‐SH3 domain we show that this interaction probably takes place between the RT‐ and distal loops. Thus, the Pex13p‐SH3–Pex5p interaction establishes a novel mode of SH3 interaction.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/19.23.6382</identifier><identifier>PMID: 11101511</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Alanine - metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Binding, Competitive ; Cell Division ; Dose-Response Relationship, Drug ; Escherichia coli - metabolism ; Glutathione Transferase - metabolism ; Ligands ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peroxisome-Targeting Signal 1 Receptor ; peroxisomes ; Peroxisomes - metabolism ; Pex13p ; Pex5p ; Proline - metabolism ; Protein Binding ; Protein Structure, Secondary ; protein-protein interaction ; Receptors, Cytoplasmic and Nuclear - chemistry ; Receptors, Cytoplasmic and Nuclear - genetics ; Receptors, Cytoplasmic and Nuclear - metabolism ; Recombinant Fusion Proteins - metabolism ; Sequence Homology, Amino Acid ; SH3 ; src Homology Domains ; Suppression, Genetic ; Two-Hybrid System Techniques</subject><ispartof>The EMBO journal, 2000-12, Vol.19 (23), p.6382-6391</ispartof><rights>European Molecular Biology Organization 2000</rights><rights>Copyright © 2000 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Dec 01, 2000</rights><rights>Copyright © 2000 European Molecular Biology Organization 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6361-d06e002fe4b5c9c2533afa93494899bd6abd7758254459b9c64c29f4aa2c9d3</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/PMC305852/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC305852/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27922,27923,53789,53791</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11101511$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Barnett, Phil</creatorcontrib><creatorcontrib>Bottger, Gina</creatorcontrib><creatorcontrib>Klein, André T.J.</creatorcontrib><creatorcontrib>Tabak, Henk F.</creatorcontrib><creatorcontrib>Distel, Ben</creatorcontrib><title>The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Src homology 3 (SH3) domains are small non‐catalytic protein modules capable of mediating protein–protein interactions by binding to proline‐X‐X‐proline (P‐X‐X‐P) motifs. Here we demonstrate that the SH3 domain of the integral peroxisomal membrane protein Pex13p is able to bind two proteins, one of which, Pex5p, represents a novel non‐P‐X‐X‐P ligand. Using alanine scanning, two‐hybrid and
in vitro
interaction analysis, we show that an α‐helical element in Pex5p is necessary and sufficient for SH3 interaction. Sup pressor analysis using Pex5p mutants located in this α‐helical element allowed the identification of a unique site of interaction for Pex5p on the Pex13p‐SH3 domain that is distinct from the classical P‐X‐X‐P binding pocket. On the basis of a structural model of the Pex13p‐SH3 domain we show that this interaction probably takes place between the RT‐ and distal loops. Thus, the Pex13p‐SH3–Pex5p interaction establishes a novel mode of SH3 interaction.</description><subject>Alanine - metabolism</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Cell Division</subject><subject>Dose-Response Relationship, Drug</subject><subject>Escherichia coli - metabolism</subject><subject>Glutathione Transferase - metabolism</subject><subject>Ligands</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Peroxisome-Targeting Signal 1 Receptor</subject><subject>peroxisomes</subject><subject>Peroxisomes - metabolism</subject><subject>Pex13p</subject><subject>Pex5p</subject><subject>Proline - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Secondary</subject><subject>protein-protein interaction</subject><subject>Receptors, Cytoplasmic and Nuclear - chemistry</subject><subject>Receptors, Cytoplasmic and Nuclear - genetics</subject><subject>Receptors, Cytoplasmic and Nuclear - metabolism</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>SH3</subject><subject>src Homology Domains</subject><subject>Suppression, Genetic</subject><subject>Two-Hybrid System Techniques</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqFkM1vEzEQxS1ERUPLnQvI4r6pP3fXBw40Ki00LaBWytHy7s42Dlk72Js2_e9x2CgtB8TJkuf93rx5CL2lZEyJ4ifQVX5xQtWY8XHOS_YCjajIScZIIV-iEWE5zQQt1SF6HeOCECLLgr5Ch5RSQiWlI3R1Owe8guA3NvrOLHGXPINx6TP4HqzD32FD-QrHuX-I2GDn7yGpfAPYt_jmgmPregim7q13x-igNcsIb3bvEbr5fHY7ucim386_TD5NszrnKVJDciCEtSAqWauaSc5NaxQXSpRKVU1uqqYoZMmkEFJVqs5FzVQrjGG1avgR-ji4rtZVB00Nrg9mqVfBdiY8am-s_nvi7Fzf-XvN0_2SJf7Djg_-1xpirxd-HVwKrKmSaalkZRKRQVQHH2OAdu9Pid6Wr_-UnwjNuN6Wn5D3z3M9Abu2k0ANgge7hMf_Guqzq9OvhUy9yC1LBzYmzN1BeBb634HeDYwz_TrAfuGTZzbMbexhsx-b8FPnBS-knl2f62J6OZOTWal_8N8QhbxK</recordid><startdate>20001201</startdate><enddate>20001201</enddate><creator>Barnett, Phil</creator><creator>Bottger, Gina</creator><creator>Klein, André T.J.</creator><creator>Tabak, Henk F.</creator><creator>Distel, Ben</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><scope>BSCLL</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20001201</creationdate><title>The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction</title><author>Barnett, Phil ; Bottger, Gina ; Klein, André T.J. ; Tabak, Henk F. ; Distel, Ben</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6361-d06e002fe4b5c9c2533afa93494899bd6abd7758254459b9c64c29f4aa2c9d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Alanine - metabolism</topic><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>Cell Division</topic><topic>Dose-Response Relationship, Drug</topic><topic>Escherichia coli - metabolism</topic><topic>Glutathione Transferase - metabolism</topic><topic>Ligands</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Peroxisome-Targeting Signal 1 Receptor</topic><topic>peroxisomes</topic><topic>Peroxisomes - metabolism</topic><topic>Pex13p</topic><topic>Pex5p</topic><topic>Proline - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Secondary</topic><topic>protein-protein interaction</topic><topic>Receptors, Cytoplasmic and Nuclear - chemistry</topic><topic>Receptors, Cytoplasmic and Nuclear - genetics</topic><topic>Receptors, Cytoplasmic and Nuclear - metabolism</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>SH3</topic><topic>src Homology Domains</topic><topic>Suppression, Genetic</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barnett, Phil</creatorcontrib><creatorcontrib>Bottger, Gina</creatorcontrib><creatorcontrib>Klein, André T.J.</creatorcontrib><creatorcontrib>Tabak, Henk F.</creatorcontrib><creatorcontrib>Distel, Ben</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>ProQuest - Health & Medical Complete保健、医学与药学数据库</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest research library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Barnett, Phil</au><au>Bottger, Gina</au><au>Klein, André T.J.</au><au>Tabak, Henk F.</au><au>Distel, Ben</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2000-12-01</date><risdate>2000</risdate><volume>19</volume><issue>23</issue><spage>6382</spage><epage>6391</epage><pages>6382-6391</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Src homology 3 (SH3) domains are small non‐catalytic protein modules capable of mediating protein–protein interactions by binding to proline‐X‐X‐proline (P‐X‐X‐P) motifs. Here we demonstrate that the SH3 domain of the integral peroxisomal membrane protein Pex13p is able to bind two proteins, one of which, Pex5p, represents a novel non‐P‐X‐X‐P ligand. Using alanine scanning, two‐hybrid and
in vitro
interaction analysis, we show that an α‐helical element in Pex5p is necessary and sufficient for SH3 interaction. Sup pressor analysis using Pex5p mutants located in this α‐helical element allowed the identification of a unique site of interaction for Pex5p on the Pex13p‐SH3 domain that is distinct from the classical P‐X‐X‐P binding pocket. On the basis of a structural model of the Pex13p‐SH3 domain we show that this interaction probably takes place between the RT‐ and distal loops. Thus, the Pex13p‐SH3–Pex5p interaction establishes a novel mode of SH3 interaction.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>11101511</pmid><doi>10.1093/emboj/19.23.6382</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0261-4189 |
| ispartof | The EMBO journal, 2000-12, Vol.19 (23), p.6382-6391 |
| issn | 0261-4189 1460-2075 1460-2075 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_305852 |
| source | PubMed Central (PMC) |
| subjects | Alanine - metabolism Amino Acid Motifs Amino Acid Sequence Binding Sites Binding, Competitive Cell Division Dose-Response Relationship, Drug Escherichia coli - metabolism Glutathione Transferase - metabolism Ligands Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Peroxisome-Targeting Signal 1 Receptor peroxisomes Peroxisomes - metabolism Pex13p Pex5p Proline - metabolism Protein Binding Protein Structure, Secondary protein-protein interaction Receptors, Cytoplasmic and Nuclear - chemistry Receptors, Cytoplasmic and Nuclear - genetics Receptors, Cytoplasmic and Nuclear - metabolism Recombinant Fusion Proteins - metabolism Sequence Homology, Amino Acid SH3 src Homology Domains Suppression, Genetic Two-Hybrid System Techniques |
| title | The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T10%3A03%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20peroxisomal%20membrane%20protein%20Pex13p%20shows%20a%20novel%20mode%20of%20SH3%20interaction&rft.jtitle=The%20EMBO%20journal&rft.au=Barnett,%20Phil&rft.date=2000-12-01&rft.volume=19&rft.issue=23&rft.spage=6382&rft.epage=6391&rft.pages=6382-6391&rft.issn=0261-4189&rft.eissn=1460-2075&rft.coden=EMJODG&rft_id=info:doi/10.1093/emboj/19.23.6382&rft_dat=%3Cproquest_pubme%3E374524891%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c6361-d06e002fe4b5c9c2533afa93494899bd6abd7758254459b9c64c29f4aa2c9d3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=195254528&rft_id=info:pmid/11101511&rfr_iscdi=true |