Identifying Pex21p as a protein that specifically interacts with yeast seryl-tRNA synthetase
The interaction of Saccharomyces cerevisiae seryl-tRNA synthetase (SerRS) with peroxin Pex21p was identified in a two-hybrid screen with SerRS as bait. This was confirmed by an in vitro binding assay with truncated Pex21p fused to glutathione S-transferase. Furthermore, purified Pex21p acts as an ac...
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| Veröffentlicht in: | FEMS microbiology letters 2002-08, Vol.214 (1), p.101-106 |
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| creator | Rocak, S Landeka, I Weygand-Durasevic, I |
| description | The interaction of Saccharomyces cerevisiae seryl-tRNA synthetase (SerRS) with peroxin Pex21p was identified in a two-hybrid screen with SerRS as bait. This was confirmed by an in vitro binding assay with truncated Pex21p fused to glutathione S-transferase. Furthermore, purified Pex21p acts as an activator of yeast seryl-tRNA synthetase in aminoacylation in vitro, revealing the functional significance of the Pex21p-SerRS interaction. Pex21p is a protein involved in the peroxisome biogenesis [Purdue, P.E., Yang, X. and Lazarow, P.B., J. Cell Biol. 143 (1998) 1859-1869]. Since eukaryotic aminoacyl-tRNA synthetases are known to participate in assembles with other synthetases and non-synthetase proteins, we propose that this unusual interaction reflects another function of the peroxin. |
| doi_str_mv | 10.1111/j.1574-6968.2002.tb11331.x |
| format | Article |
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This was confirmed by an in vitro binding assay with truncated Pex21p fused to glutathione S-transferase. Furthermore, purified Pex21p acts as an activator of yeast seryl-tRNA synthetase in aminoacylation in vitro, revealing the functional significance of the Pex21p-SerRS interaction. Pex21p is a protein involved in the peroxisome biogenesis [Purdue, P.E., Yang, X. and Lazarow, P.B., J. Cell Biol. 143 (1998) 1859-1869]. Since eukaryotic aminoacyl-tRNA synthetases are known to participate in assembles with other synthetases and non-synthetase proteins, we propose that this unusual interaction reflects another function of the peroxin.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2002.tb11331.x</identifier><identifier>PMID: 12204379</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>aminoacyl tRNA ligases ; Aminoacylation ; Aminoacyl‐tRNA synthetase ; Baits ; Baking yeast ; biogenesis ; Biological and medical sciences ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Glutathione ; Glutathione transferase ; Glutathione Transferase - genetics ; Glutathione Transferase - metabolism ; Growth, nutrition, metabolism, transports, enzymes. Molecular biology ; Microbiology ; Mycology ; Peroxin ; Protein Binding ; Protein synthesis ; Proteins ; Protein–protein interactions ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Serine-tRNA ligase ; Serine-tRNA Ligase - metabolism ; tRNA ; Two-Hybrid System Techniques ; two‐hybrid system ; Yeasts</subject><ispartof>FEMS microbiology letters, 2002-08, Vol.214 (1), p.101-106</ispartof><rights>2002 Federation of European Microbiological Societies 2002</rights><rights>2002 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5131-167e827679ef56ece117f6edb7b54c3de119c7de16e5ac30dc1dc2f14c11b8553</citedby><cites>FETCH-LOGICAL-c5131-167e827679ef56ece117f6edb7b54c3de119c7de16e5ac30dc1dc2f14c11b8553</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2002.tb11331.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2002.tb11331.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14655235$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12204379$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rocak, S</creatorcontrib><creatorcontrib>Landeka, I</creatorcontrib><creatorcontrib>Weygand-Durasevic, I</creatorcontrib><title>Identifying Pex21p as a protein that specifically interacts with yeast seryl-tRNA synthetase</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>The interaction of Saccharomyces cerevisiae seryl-tRNA synthetase (SerRS) with peroxin Pex21p was identified in a two-hybrid screen with SerRS as bait. This was confirmed by an in vitro binding assay with truncated Pex21p fused to glutathione S-transferase. Furthermore, purified Pex21p acts as an activator of yeast seryl-tRNA synthetase in aminoacylation in vitro, revealing the functional significance of the Pex21p-SerRS interaction. Pex21p is a protein involved in the peroxisome biogenesis [Purdue, P.E., Yang, X. and Lazarow, P.B., J. Cell Biol. 143 (1998) 1859-1869]. Since eukaryotic aminoacyl-tRNA synthetases are known to participate in assembles with other synthetases and non-synthetase proteins, we propose that this unusual interaction reflects another function of the peroxin.</description><subject>aminoacyl tRNA ligases</subject><subject>Aminoacylation</subject><subject>Aminoacyl‐tRNA synthetase</subject><subject>Baits</subject><subject>Baking yeast</subject><subject>biogenesis</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glutathione</subject><subject>Glutathione transferase</subject><subject>Glutathione Transferase - genetics</subject><subject>Glutathione Transferase - metabolism</subject><subject>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</subject><subject>Microbiology</subject><subject>Mycology</subject><subject>Peroxin</subject><subject>Protein Binding</subject><subject>Protein synthesis</subject><subject>Proteins</subject><subject>Protein–protein interactions</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Serine-tRNA ligase</subject><subject>Serine-tRNA Ligase - metabolism</subject><subject>tRNA</subject><subject>Two-Hybrid System Techniques</subject><subject>two‐hybrid system</subject><subject>Yeasts</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqVkl-L1DAUxYso7rj6FTQo-taam7RJuw_Csri6MP5B3TchpOntToZOW5uUnX57U1pcEEXMyyXkd27uyUkUPQeaQFiv9wlkMo1FIfKEUcoSXwJwDsnxXrT5dXQ_2lAu8xhoIU-iR87tKaUpo-JhdAKM0ZTLYhN9v6qw9baebHtDPuORQU-0I5r0Q-fRtsTvtCeuR2Nra3TTTMS2HgdtvCO31u_IhNoFAoepif2Xj-fETa3fodcOH0cPat04fLLW0-j68u23i_fx9tO7q4vzbWwy4BCDkJgzKWSBdSbQIICsBValLLPU8CrsCyNDEZhpw2lloDKshtQAlHmW8dPo1dI3DP1jROfVwTqDTaNb7EanZHALjMt_gpCnOWeCBvDFb-C-G4c2mFCMAxUShMgDdbZQZuicG7BW_WAPepgUUDVHpfZqzkPNeag5KrVGpY5B_HS9YiwPWN1J12wC8HIFtAsvXw-6NdbdcanIMsZn928W7tY2OP3HCOrywxYohAbZ0qAb-7_I4z87eLboat0pfTOE4a6_MgoifLRCyiLnPwHMs8kY</recordid><startdate>20020827</startdate><enddate>20020827</enddate><creator>Rocak, S</creator><creator>Landeka, I</creator><creator>Weygand-Durasevic, I</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</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>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</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>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20020827</creationdate><title>Identifying Pex21p as a protein that specifically interacts with yeast seryl-tRNA synthetase</title><author>Rocak, S ; Landeka, I ; Weygand-Durasevic, I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5131-167e827679ef56ece117f6edb7b54c3de119c7de16e5ac30dc1dc2f14c11b8553</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>aminoacyl tRNA ligases</topic><topic>Aminoacylation</topic><topic>Aminoacyl‐tRNA synthetase</topic><topic>Baits</topic><topic>Baking yeast</topic><topic>biogenesis</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glutathione</topic><topic>Glutathione transferase</topic><topic>Glutathione Transferase - genetics</topic><topic>Glutathione Transferase - metabolism</topic><topic>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</topic><topic>Microbiology</topic><topic>Mycology</topic><topic>Peroxin</topic><topic>Protein Binding</topic><topic>Protein synthesis</topic><topic>Proteins</topic><topic>Protein–protein interactions</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Serine-tRNA ligase</topic><topic>Serine-tRNA Ligase - metabolism</topic><topic>tRNA</topic><topic>Two-Hybrid System Techniques</topic><topic>two‐hybrid system</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rocak, S</creatorcontrib><creatorcontrib>Landeka, I</creatorcontrib><creatorcontrib>Weygand-Durasevic, I</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rocak, S</au><au>Landeka, I</au><au>Weygand-Durasevic, I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identifying Pex21p as a protein that specifically interacts with yeast seryl-tRNA synthetase</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2002-08-27</date><risdate>2002</risdate><volume>214</volume><issue>1</issue><spage>101</spage><epage>106</epage><pages>101-106</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>The interaction of Saccharomyces cerevisiae seryl-tRNA synthetase (SerRS) with peroxin Pex21p was identified in a two-hybrid screen with SerRS as bait. This was confirmed by an in vitro binding assay with truncated Pex21p fused to glutathione S-transferase. Furthermore, purified Pex21p acts as an activator of yeast seryl-tRNA synthetase in aminoacylation in vitro, revealing the functional significance of the Pex21p-SerRS interaction. Pex21p is a protein involved in the peroxisome biogenesis [Purdue, P.E., Yang, X. and Lazarow, P.B., J. Cell Biol. 143 (1998) 1859-1869]. Since eukaryotic aminoacyl-tRNA synthetases are known to participate in assembles with other synthetases and non-synthetase proteins, we propose that this unusual interaction reflects another function of the peroxin.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>12204379</pmid><doi>10.1111/j.1574-6968.2002.tb11331.x</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEMS microbiology letters, 2002-08, Vol.214 (1), p.101-106 |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | aminoacyl tRNA ligases Aminoacylation Aminoacyl‐tRNA synthetase Baits Baking yeast biogenesis Biological and medical sciences Carrier Proteins - genetics Carrier Proteins - metabolism Fundamental and applied biological sciences. Psychology Glutathione Glutathione transferase Glutathione Transferase - genetics Glutathione Transferase - metabolism Growth, nutrition, metabolism, transports, enzymes. Molecular biology Microbiology Mycology Peroxin Protein Binding Protein synthesis Proteins Protein–protein interactions Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Serine-tRNA ligase Serine-tRNA Ligase - metabolism tRNA Two-Hybrid System Techniques two‐hybrid system Yeasts |
| title | Identifying Pex21p as a protein that specifically interacts with yeast seryl-tRNA synthetase |
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