Toward a Protein-Protein Interaction Map of the budding Yeast: A Comprehensive System to Examine Two-Hybrid Interactions in All Possible Combinations between the Yeast Proteins
Protein-protein interactions play pivotal roles in various aspects of the structural and functional organization of the cell, and their complete description is indispensable to thorough understanding of the cell. As an approach toward this goal, here we report a comprehensive system to examine two-h...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2000-02, Vol.97 (3), p.1143-1147 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1147 |
|---|---|
| container_issue | 3 |
| container_start_page | 1143 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 97 |
| creator | Ito, Takashi Tashiro, Kosuke Muta, Shigeru Ozawa, Ritsuko Chiba, Tomoko Nishizawa, Mayumi Yamamoto, Kiyoshi Kuhara, Satoru Sakaki, Yoshiyuki |
| description | Protein-protein interactions play pivotal roles in various aspects of the structural and functional organization of the cell, and their complete description is indispensable to thorough understanding of the cell. As an approach toward this goal, here we report a comprehensive system to examine two-hybrid interactions in all of the possible combinations between proteins of Saccharomyces cerevisiae. We cloned all of the yeast ORFs individually as a DNA-binding domain fusion ("bait") in a MATa strain and as an activation domain fusion ("prey") in a MATα strain, and subsequently divided them into pools, each containing 96 clones. These bait and prey clone pools were systematically mated with each other, and the transformants were subjected to strict selection for the activation of three reporter genes followed by sequence tagging. Our initial examination of ≈ 4× 106different combinations, constituting ≈ 10% of the total to be tested, has revealed 183 independent two-hybrid interactions, more than half of which are entirely novel. Notably, the obtained binary data allow us to extract more complex interaction networks, including the one that may explain a currently unsolved mechanism for the connection between distinct steps of vesicular transport. The approach described here thus will provide many leads for integration of various cellular functions and serve as a major driving force in the completion of the protein-protein interaction map. |
| doi_str_mv | 10.1073/pnas.97.3.1143 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_70883690</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>121620</jstor_id><sourcerecordid>121620</sourcerecordid><originalsourceid>FETCH-LOGICAL-c581t-880661edfa69bbc6e8724605673a1cef7d676882b02a29ab138133545bebcfbb3</originalsourceid><addsrcrecordid>eNqFkkFv1DAQhSMEokvhygWBLA69Jdhx4jiIy2pVaKUiKrEcOFl2Mul6ldip7XS7_6o_sUl3CwsHkCzNYb73Zjx6UfSa4ITggn7ojfRJWSQ0ISSjT6IZwSWJWVbip9EM47SIeZZmR9EL79cY4zLn-Hl0RDDL86zks-huaTfS1UiiS2cDaBPvKzo3AZysgrYGfZU9sg0KK0BqqGttrtBPkD58RHO0sF3vYAXG6xtA37c-QIeCRae3stMG0HJj47Otcro-tPRoHDFvW3RpvdeqhclHaSN3TQVhA2AeJj5MelzPv4yeNbL18Gpfj6Mfn0-Xi7P44tuX88X8Iq5yTkLMOWaMQN1IVipVMeBFmjGcs4JKUkFT1KxgnKcKpzItpSKUE0rzLFegqkYpehx92vn2g-qgrsAEJ1vRO91JtxVWavFnx-iVuLI3guR5jkf5yV7u7PUAPohO-wraVhqwgxcF5pyy8v8gKTJWjm8E3_8Fru3gzHgDkWJCGeMpGaFkB1VuvKuD5tfCBIspMGIKjCgLQcUUmFHw7vCbB_guISPwdg9Mwsf2ocHJv_qiGdo2wG0YwTc7cO2Ddb8HpYSlmN4DYZPgsg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201366821</pqid></control><display><type>article</type><title>Toward a Protein-Protein Interaction Map of the budding Yeast: A Comprehensive System to Examine Two-Hybrid Interactions in All Possible Combinations between the Yeast Proteins</title><source>MEDLINE</source><source>Jstor Complete Legacy</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Ito, Takashi ; Tashiro, Kosuke ; Muta, Shigeru ; Ozawa, Ritsuko ; Chiba, Tomoko ; Nishizawa, Mayumi ; Yamamoto, Kiyoshi ; Kuhara, Satoru ; Sakaki, Yoshiyuki</creator><creatorcontrib>Ito, Takashi ; Tashiro, Kosuke ; Muta, Shigeru ; Ozawa, Ritsuko ; Chiba, Tomoko ; Nishizawa, Mayumi ; Yamamoto, Kiyoshi ; Kuhara, Satoru ; Sakaki, Yoshiyuki</creatorcontrib><description>Protein-protein interactions play pivotal roles in various aspects of the structural and functional organization of the cell, and their complete description is indispensable to thorough understanding of the cell. As an approach toward this goal, here we report a comprehensive system to examine two-hybrid interactions in all of the possible combinations between proteins of Saccharomyces cerevisiae. We cloned all of the yeast ORFs individually as a DNA-binding domain fusion ("bait") in a MATa strain and as an activation domain fusion ("prey") in a MATα strain, and subsequently divided them into pools, each containing 96 clones. These bait and prey clone pools were systematically mated with each other, and the transformants were subjected to strict selection for the activation of three reporter genes followed by sequence tagging. Our initial examination of ≈ 4× 106different combinations, constituting ≈ 10% of the total to be tested, has revealed 183 independent two-hybrid interactions, more than half of which are entirely novel. Notably, the obtained binary data allow us to extract more complex interaction networks, including the one that may explain a currently unsolved mechanism for the connection between distinct steps of vesicular transport. The approach described here thus will provide many leads for integration of various cellular functions and serve as a major driving force in the completion of the protein-protein interaction map.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.97.3.1143</identifier><identifier>PMID: 10655498</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Biological Sciences ; DNA, Fungal - genetics ; DNA, Recombinant - genetics ; Feasibility Studies ; Fungal proteins ; Fungal Proteins - physiology ; Genes, Fungal ; Genes, Reporter ; Genetic screening ; Genetics ; Genomes ; Genomics ; Open Reading Frames ; Plasmids ; Polymerase Chain Reaction ; Proteins ; Reporter genes ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Two-Hybrid System Techniques ; Yeast ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2000-02, Vol.97 (3), p.1143-1147</ispartof><rights>Copyright 1993-2000 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Feb 1, 2000</rights><rights>Copyright © 2000, The National Academy of Sciences 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c581t-880661edfa69bbc6e8724605673a1cef7d676882b02a29ab138133545bebcfbb3</citedby><cites>FETCH-LOGICAL-c581t-880661edfa69bbc6e8724605673a1cef7d676882b02a29ab138133545bebcfbb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/97/3.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/121620$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/121620$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53770,53772,57996,58229</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10655498$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ito, Takashi</creatorcontrib><creatorcontrib>Tashiro, Kosuke</creatorcontrib><creatorcontrib>Muta, Shigeru</creatorcontrib><creatorcontrib>Ozawa, Ritsuko</creatorcontrib><creatorcontrib>Chiba, Tomoko</creatorcontrib><creatorcontrib>Nishizawa, Mayumi</creatorcontrib><creatorcontrib>Yamamoto, Kiyoshi</creatorcontrib><creatorcontrib>Kuhara, Satoru</creatorcontrib><creatorcontrib>Sakaki, Yoshiyuki</creatorcontrib><title>Toward a Protein-Protein Interaction Map of the budding Yeast: A Comprehensive System to Examine Two-Hybrid Interactions in All Possible Combinations between the Yeast Proteins</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Protein-protein interactions play pivotal roles in various aspects of the structural and functional organization of the cell, and their complete description is indispensable to thorough understanding of the cell. As an approach toward this goal, here we report a comprehensive system to examine two-hybrid interactions in all of the possible combinations between proteins of Saccharomyces cerevisiae. We cloned all of the yeast ORFs individually as a DNA-binding domain fusion ("bait") in a MATa strain and as an activation domain fusion ("prey") in a MATα strain, and subsequently divided them into pools, each containing 96 clones. These bait and prey clone pools were systematically mated with each other, and the transformants were subjected to strict selection for the activation of three reporter genes followed by sequence tagging. Our initial examination of ≈ 4× 106different combinations, constituting ≈ 10% of the total to be tested, has revealed 183 independent two-hybrid interactions, more than half of which are entirely novel. Notably, the obtained binary data allow us to extract more complex interaction networks, including the one that may explain a currently unsolved mechanism for the connection between distinct steps of vesicular transport. The approach described here thus will provide many leads for integration of various cellular functions and serve as a major driving force in the completion of the protein-protein interaction map.</description><subject>Biological Sciences</subject><subject>DNA, Fungal - genetics</subject><subject>DNA, Recombinant - genetics</subject><subject>Feasibility Studies</subject><subject>Fungal proteins</subject><subject>Fungal Proteins - physiology</subject><subject>Genes, Fungal</subject><subject>Genes, Reporter</subject><subject>Genetic screening</subject><subject>Genetics</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Open Reading Frames</subject><subject>Plasmids</subject><subject>Polymerase Chain Reaction</subject><subject>Proteins</subject><subject>Reporter genes</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Two-Hybrid System Techniques</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkkFv1DAQhSMEokvhygWBLA69Jdhx4jiIy2pVaKUiKrEcOFl2Mul6ldip7XS7_6o_sUl3CwsHkCzNYb73Zjx6UfSa4ITggn7ojfRJWSQ0ISSjT6IZwSWJWVbip9EM47SIeZZmR9EL79cY4zLn-Hl0RDDL86zks-huaTfS1UiiS2cDaBPvKzo3AZysgrYGfZU9sg0KK0BqqGttrtBPkD58RHO0sF3vYAXG6xtA37c-QIeCRae3stMG0HJj47Otcro-tPRoHDFvW3RpvdeqhclHaSN3TQVhA2AeJj5MelzPv4yeNbL18Gpfj6Mfn0-Xi7P44tuX88X8Iq5yTkLMOWaMQN1IVipVMeBFmjGcs4JKUkFT1KxgnKcKpzItpSKUE0rzLFegqkYpehx92vn2g-qgrsAEJ1vRO91JtxVWavFnx-iVuLI3guR5jkf5yV7u7PUAPohO-wraVhqwgxcF5pyy8v8gKTJWjm8E3_8Fru3gzHgDkWJCGeMpGaFkB1VuvKuD5tfCBIspMGIKjCgLQcUUmFHw7vCbB_guISPwdg9Mwsf2ocHJv_qiGdo2wG0YwTc7cO2Ddb8HpYSlmN4DYZPgsg</recordid><startdate>20000201</startdate><enddate>20000201</enddate><creator>Ito, Takashi</creator><creator>Tashiro, Kosuke</creator><creator>Muta, Shigeru</creator><creator>Ozawa, Ritsuko</creator><creator>Chiba, Tomoko</creator><creator>Nishizawa, Mayumi</creator><creator>Yamamoto, Kiyoshi</creator><creator>Kuhara, Satoru</creator><creator>Sakaki, Yoshiyuki</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><general>The National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000201</creationdate><title>Toward a Protein-Protein Interaction Map of the budding Yeast: A Comprehensive System to Examine Two-Hybrid Interactions in All Possible Combinations between the Yeast Proteins</title><author>Ito, Takashi ; Tashiro, Kosuke ; Muta, Shigeru ; Ozawa, Ritsuko ; Chiba, Tomoko ; Nishizawa, Mayumi ; Yamamoto, Kiyoshi ; Kuhara, Satoru ; Sakaki, Yoshiyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c581t-880661edfa69bbc6e8724605673a1cef7d676882b02a29ab138133545bebcfbb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Biological Sciences</topic><topic>DNA, Fungal - genetics</topic><topic>DNA, Recombinant - genetics</topic><topic>Feasibility Studies</topic><topic>Fungal proteins</topic><topic>Fungal Proteins - physiology</topic><topic>Genes, Fungal</topic><topic>Genes, Reporter</topic><topic>Genetic screening</topic><topic>Genetics</topic><topic>Genomes</topic><topic>Genomics</topic><topic>Open Reading Frames</topic><topic>Plasmids</topic><topic>Polymerase Chain Reaction</topic><topic>Proteins</topic><topic>Reporter genes</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Two-Hybrid System Techniques</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ito, Takashi</creatorcontrib><creatorcontrib>Tashiro, Kosuke</creatorcontrib><creatorcontrib>Muta, Shigeru</creatorcontrib><creatorcontrib>Ozawa, Ritsuko</creatorcontrib><creatorcontrib>Chiba, Tomoko</creatorcontrib><creatorcontrib>Nishizawa, Mayumi</creatorcontrib><creatorcontrib>Yamamoto, Kiyoshi</creatorcontrib><creatorcontrib>Kuhara, Satoru</creatorcontrib><creatorcontrib>Sakaki, Yoshiyuki</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</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>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ito, Takashi</au><au>Tashiro, Kosuke</au><au>Muta, Shigeru</au><au>Ozawa, Ritsuko</au><au>Chiba, Tomoko</au><au>Nishizawa, Mayumi</au><au>Yamamoto, Kiyoshi</au><au>Kuhara, Satoru</au><au>Sakaki, Yoshiyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Toward a Protein-Protein Interaction Map of the budding Yeast: A Comprehensive System to Examine Two-Hybrid Interactions in All Possible Combinations between the Yeast Proteins</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2000-02-01</date><risdate>2000</risdate><volume>97</volume><issue>3</issue><spage>1143</spage><epage>1147</epage><pages>1143-1147</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Protein-protein interactions play pivotal roles in various aspects of the structural and functional organization of the cell, and their complete description is indispensable to thorough understanding of the cell. As an approach toward this goal, here we report a comprehensive system to examine two-hybrid interactions in all of the possible combinations between proteins of Saccharomyces cerevisiae. We cloned all of the yeast ORFs individually as a DNA-binding domain fusion ("bait") in a MATa strain and as an activation domain fusion ("prey") in a MATα strain, and subsequently divided them into pools, each containing 96 clones. These bait and prey clone pools were systematically mated with each other, and the transformants were subjected to strict selection for the activation of three reporter genes followed by sequence tagging. Our initial examination of ≈ 4× 106different combinations, constituting ≈ 10% of the total to be tested, has revealed 183 independent two-hybrid interactions, more than half of which are entirely novel. Notably, the obtained binary data allow us to extract more complex interaction networks, including the one that may explain a currently unsolved mechanism for the connection between distinct steps of vesicular transport. The approach described here thus will provide many leads for integration of various cellular functions and serve as a major driving force in the completion of the protein-protein interaction map.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>10655498</pmid><doi>10.1073/pnas.97.3.1143</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2000-02, Vol.97 (3), p.1143-1147 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70883690 |
| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Biological Sciences DNA, Fungal - genetics DNA, Recombinant - genetics Feasibility Studies Fungal proteins Fungal Proteins - physiology Genes, Fungal Genes, Reporter Genetic screening Genetics Genomes Genomics Open Reading Frames Plasmids Polymerase Chain Reaction Proteins Reporter genes Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Two-Hybrid System Techniques Yeast Yeasts |
| title | Toward a Protein-Protein Interaction Map of the budding Yeast: A Comprehensive System to Examine Two-Hybrid Interactions in All Possible Combinations between the Yeast Proteins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T14%3A01%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Toward%20a%20Protein-Protein%20Interaction%20Map%20of%20the%20budding%20Yeast:%20A%20Comprehensive%20System%20to%20Examine%20Two-Hybrid%20Interactions%20in%20All%20Possible%20Combinations%20between%20the%20Yeast%20Proteins&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Ito,%20Takashi&rft.date=2000-02-01&rft.volume=97&rft.issue=3&rft.spage=1143&rft.epage=1147&rft.pages=1143-1147&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.97.3.1143&rft_dat=%3Cjstor_proqu%3E121620%3C/jstor_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=201366821&rft_id=info:pmid/10655498&rft_jstor_id=121620&rfr_iscdi=true |