Yeast NPI46 Encodes a Novel Prolyl cis-trans Isomerase That Is Located in the Nucleolus
We have identified a gene (NPI46) encoding a new prolyl cis-trans isomerase within the nucleolus of the yeast Saccharomyces cerevisiae. The protein encoded by NPI46 was originally found by us in a search for proteins that recognize nuclear localization sequences (NLSs) in vitro. Thus, NPI46 binds to...
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| Veröffentlicht in: | The Journal of cell biology 1994-08, Vol.126 (4), p.853-862 |
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| container_title | The Journal of cell biology |
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| creator | Shan, Xiaoyin Xue, Zhixiong Mélèse, Teri |
| description | We have identified a gene (NPI46) encoding a new prolyl cis-trans isomerase within the nucleolus of the yeast Saccharomyces cerevisiae. The protein encoded by NPI46 was originally found by us in a search for proteins that recognize nuclear localization sequences (NLSs) in vitro. Thus, NPI46 binds to affinity columns that contain a wild-type histone H2B NLS but not a mutant H2B NLS that is incompetent for nuclear localization in vivo. NPI46 has two domains, a highly charged NH2 terminus similar to two other mammalian nucleolar proteins, nucleolin and Nopp140, and a COOH terminus with 45% homology to a family of mammalian and yeast proline isomerases. NPI46 is capable of catalyzing the prolyl cis-trans isomerization of two small synthetic peptides, succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, as measured by a chymotrypsin-coupled spectrophotometric assay. By indirect immunofluorescence we have shown that NPI46 is a nucleolar protein. NPI46 is not essential for cell viability. |
| doi_str_mv | 10.1083/jcb.126.4.853 |
| format | Article |
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The protein encoded by NPI46 was originally found by us in a search for proteins that recognize nuclear localization sequences (NLSs) in vitro. Thus, NPI46 binds to affinity columns that contain a wild-type histone H2B NLS but not a mutant H2B NLS that is incompetent for nuclear localization in vivo. NPI46 has two domains, a highly charged NH2 terminus similar to two other mammalian nucleolar proteins, nucleolin and Nopp140, and a COOH terminus with 45% homology to a family of mammalian and yeast proline isomerases. NPI46 is capable of catalyzing the prolyl cis-trans isomerization of two small synthetic peptides, succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, as measured by a chymotrypsin-coupled spectrophotometric assay. By indirect immunofluorescence we have shown that NPI46 is a nucleolar protein. NPI46 is not essential for cell viability.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.126.4.853</identifier><identifier>PMID: 8051210</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>New York, NY: Rockefeller University Press</publisher><subject>Amino Acid Isomerases - biosynthesis ; Amino Acid Isomerases - genetics ; Amino Acid Isomerases - isolation & purification ; Amino Acid Sequence ; Animals ; Antibodies ; Base Sequence ; Biological and medical sciences ; Carrier Proteins - biosynthesis ; Carrier Proteins - genetics ; Carrier Proteins - isolation & purification ; Cell Nucleolus - enzymology ; Cells ; Chromatography, Affinity ; Cloning, Molecular ; DNA, Fungal - isolation & purification ; DNA, Fungal - metabolism ; Enzymes ; Epitopes ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Genes ; Genes, Fungal ; Goods and services tax ; India ink ; Kinetics ; Mammals ; Mice ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Nuclear proteins ; Oligopeptides - metabolism ; Peptidylprolyl Isomerase ; Plasmids ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Sequence Homology, Amino Acid ; Substrate Specificity ; Yeasts</subject><ispartof>The Journal of cell biology, 1994-08, Vol.126 (4), p.853-862</ispartof><rights>Copyright 1994 The Rockefeller University Press</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3783-35ec9f2fcf92dd9645e7c6fbe5af3debd96afccd1fdf9290cba012455ce0a1623</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4239593$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8051210$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shan, Xiaoyin</creatorcontrib><creatorcontrib>Xue, Zhixiong</creatorcontrib><creatorcontrib>Mélèse, Teri</creatorcontrib><title>Yeast NPI46 Encodes a Novel Prolyl cis-trans Isomerase That Is Located in the Nucleolus</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>We have identified a gene (NPI46) encoding a new prolyl cis-trans isomerase within the nucleolus of the yeast Saccharomyces cerevisiae. The protein encoded by NPI46 was originally found by us in a search for proteins that recognize nuclear localization sequences (NLSs) in vitro. Thus, NPI46 binds to affinity columns that contain a wild-type histone H2B NLS but not a mutant H2B NLS that is incompetent for nuclear localization in vivo. NPI46 has two domains, a highly charged NH2 terminus similar to two other mammalian nucleolar proteins, nucleolin and Nopp140, and a COOH terminus with 45% homology to a family of mammalian and yeast proline isomerases. NPI46 is capable of catalyzing the prolyl cis-trans isomerization of two small synthetic peptides, succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, as measured by a chymotrypsin-coupled spectrophotometric assay. By indirect immunofluorescence we have shown that NPI46 is a nucleolar protein. NPI46 is not essential for cell viability.</description><subject>Amino Acid Isomerases - biosynthesis</subject><subject>Amino Acid Isomerases - genetics</subject><subject>Amino Acid Isomerases - isolation & purification</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - biosynthesis</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Cell Nucleolus - enzymology</subject><subject>Cells</subject><subject>Chromatography, Affinity</subject><subject>Cloning, Molecular</subject><subject>DNA, Fungal - isolation & purification</subject><subject>DNA, Fungal - metabolism</subject><subject>Enzymes</subject><subject>Epitopes</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Genes</subject><subject>Genes, Fungal</subject><subject>Goods and services tax</subject><subject>India ink</subject><subject>Kinetics</subject><subject>Mammals</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Nuclear proteins</subject><subject>Oligopeptides - metabolism</subject><subject>Peptidylprolyl Isomerase</subject><subject>Plasmids</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><subject>Yeasts</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1rGzEURUVoSd00y-wa0KJ0N46-Z7QphJAmBuNmkVK6EhrNUzxGHiXSTCD_vmps3HbVlZDu4eo9DkJnlMwpafjFxrVzytRczBvJj9CMSkGqhgryBs0IYbTSksl36H3OG0KIqAU_RscNkZRRMkM_foLNI17dLYTC14OLHWRs8So-Q8B3KYaXgF2fqzHZIeNFjltINgO-X9uxXPEyOjtCh_sBj2vAq8kFiGHKH9Bbb0OG0_15gr5_vb6_uq2W324WV5fLyvG64RWX4LRn3nnNuk4rIaF2yrcgrecdtOXJeuc66rtCaOJaSygTUjoglirGT9CXXe_j1G6hczCUSYN5TP3WphcTbW_-TYZ-bR7is2GUEUqbUvB5X5Di0wR5NNs-OwjBDhCnbGqlWE00_y9IlaoLpgtY7UCXYs4J_GEaSsxvZaYoM0WZEaYoK_z53ysc6L2jkn_a5zY7G3wxUYwcMMG4lq_zfdxhmzzG9OdPRZVoNP8FNPepDg</recordid><startdate>199408</startdate><enddate>199408</enddate><creator>Shan, Xiaoyin</creator><creator>Xue, Zhixiong</creator><creator>Mélèse, Teri</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>199408</creationdate><title>Yeast NPI46 Encodes a Novel Prolyl cis-trans Isomerase That Is Located in the Nucleolus</title><author>Shan, Xiaoyin ; Xue, Zhixiong ; Mélèse, Teri</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3783-35ec9f2fcf92dd9645e7c6fbe5af3debd96afccd1fdf9290cba012455ce0a1623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Isomerases - biosynthesis</topic><topic>Amino Acid Isomerases - genetics</topic><topic>Amino Acid Isomerases - isolation & purification</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - biosynthesis</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Cell Nucleolus - enzymology</topic><topic>Cells</topic><topic>Chromatography, Affinity</topic><topic>Cloning, Molecular</topic><topic>DNA, Fungal - isolation & purification</topic><topic>DNA, Fungal - metabolism</topic><topic>Enzymes</topic><topic>Epitopes</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Genes</topic><topic>Genes, Fungal</topic><topic>Goods and services tax</topic><topic>India ink</topic><topic>Kinetics</topic><topic>Mammals</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Nuclear proteins</topic><topic>Oligopeptides - metabolism</topic><topic>Peptidylprolyl Isomerase</topic><topic>Plasmids</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shan, Xiaoyin</creatorcontrib><creatorcontrib>Xue, Zhixiong</creatorcontrib><creatorcontrib>Mélèse, Teri</creatorcontrib><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>Technology Research Database</collection><collection>Engineering Research Database</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>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shan, Xiaoyin</au><au>Xue, Zhixiong</au><au>Mélèse, Teri</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Yeast NPI46 Encodes a Novel Prolyl cis-trans Isomerase That Is Located in the Nucleolus</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1994-08</date><risdate>1994</risdate><volume>126</volume><issue>4</issue><spage>853</spage><epage>862</epage><pages>853-862</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>We have identified a gene (NPI46) encoding a new prolyl cis-trans isomerase within the nucleolus of the yeast Saccharomyces cerevisiae. The protein encoded by NPI46 was originally found by us in a search for proteins that recognize nuclear localization sequences (NLSs) in vitro. Thus, NPI46 binds to affinity columns that contain a wild-type histone H2B NLS but not a mutant H2B NLS that is incompetent for nuclear localization in vivo. NPI46 has two domains, a highly charged NH2 terminus similar to two other mammalian nucleolar proteins, nucleolin and Nopp140, and a COOH terminus with 45% homology to a family of mammalian and yeast proline isomerases. NPI46 is capable of catalyzing the prolyl cis-trans isomerization of two small synthetic peptides, succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, as measured by a chymotrypsin-coupled spectrophotometric assay. By indirect immunofluorescence we have shown that NPI46 is a nucleolar protein. NPI46 is not essential for cell viability.</abstract><cop>New York, NY</cop><pub>Rockefeller University Press</pub><pmid>8051210</pmid><doi>10.1083/jcb.126.4.853</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of cell biology, 1994-08, Vol.126 (4), p.853-862 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Isomerases - biosynthesis Amino Acid Isomerases - genetics Amino Acid Isomerases - isolation & purification Amino Acid Sequence Animals Antibodies Base Sequence Biological and medical sciences Carrier Proteins - biosynthesis Carrier Proteins - genetics Carrier Proteins - isolation & purification Cell Nucleolus - enzymology Cells Chromatography, Affinity Cloning, Molecular DNA, Fungal - isolation & purification DNA, Fungal - metabolism Enzymes Epitopes Escherichia coli Fundamental and applied biological sciences. Psychology Gene expression Genes Genes, Fungal Goods and services tax India ink Kinetics Mammals Mice Molecular and cellular biology Molecular genetics Molecular Sequence Data Nuclear proteins Oligopeptides - metabolism Peptidylprolyl Isomerase Plasmids Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Sequence Homology, Amino Acid Substrate Specificity Yeasts |
| title | Yeast NPI46 Encodes a Novel Prolyl cis-trans Isomerase That Is Located in the Nucleolus |
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