Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins
Nup145p is an essential yeast nucleoporin involved in nuclear export of polyadenylated RNAs. We demonstrate here that Nup145p is cleaved in vivo to yield two functionally distinct domains: a carboxy‐terminal domain (C‐Nup145p) which is located at the nuclear pore complex (NPC) and assembles into the...
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| Veröffentlicht in: | The EMBO journal 1997-08, Vol.16 (16), p.5086-5097 |
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| creator | Teizeira, M.T Siniossoglou, S Podtelejnikov, S Benichou, J.C Mann, M Dujon, B Hurt, E Fabre, E |
| description | Nup145p is an essential yeast nucleoporin involved in nuclear export of polyadenylated RNAs. We demonstrate here that Nup145p is cleaved
in vivo
to yield two functionally distinct domains: a carboxy‐terminal domain (C‐Nup145p) which is located at the nuclear pore complex (NPC) and assembles into the Nup84p complex, and a GLFG‐containing amino‐terminal domain (N‐Nup145p) which is not part of this complex. Whereas the essential C‐Nup145p accomplishes the functions required for efficient mRNA export and normal NPC distribution, N‐Nup145p, which is homologous to the GLFG‐containing nucleoporins Nup100p and Nup116p, is not necessary for cell growth. However, the N‐Nup145p becomes essential in a
nup188
mutant background. Strikingly, generation of a free N‐domain is a prerequisite for complementation of this peculiar synthetic lethal mutant. These data suggest that N‐ and C‐domains of Nup145p perform independent functions, and that the
in vivo
cleavage observed is of functional importance. |
| doi_str_mv | 10.1093/emboj/16.16.5086 |
| format | Article |
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in vivo
to yield two functionally distinct domains: a carboxy‐terminal domain (C‐Nup145p) which is located at the nuclear pore complex (NPC) and assembles into the Nup84p complex, and a GLFG‐containing amino‐terminal domain (N‐Nup145p) which is not part of this complex. Whereas the essential C‐Nup145p accomplishes the functions required for efficient mRNA export and normal NPC distribution, N‐Nup145p, which is homologous to the GLFG‐containing nucleoporins Nup100p and Nup116p, is not necessary for cell growth. However, the N‐Nup145p becomes essential in a
nup188
mutant background. Strikingly, generation of a free N‐domain is a prerequisite for complementation of this peculiar synthetic lethal mutant. These data suggest that N‐ and C‐domains of Nup145p perform independent functions, and that the
in vivo
cleavage observed is of functional importance.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/16.16.5086</identifier><identifier>PMID: 9305650</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Biological Transport - physiology ; Blotting, Western ; cell membranes ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins - analysis ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; lethal mutants ; messenger RNA ; messenger rna export ; Microscopy, Electron ; Molecular Sequence Data ; mRNA export ; Mutagenesis, Site-Directed - genetics ; mutants ; Nuclear Envelope - chemistry ; Nuclear Envelope - metabolism ; nuclear membrane ; nuclear pore complex ; nuclear pore complex distribution ; Nuclear Pore Complex Proteins ; Nuclear Proteins - metabolism ; nuclei ; nucleoporin ; protein cleavage ; Protein Processing, Post-Translational ; proteins ; proteolysis ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - metabolism ; RNA, Fungal - metabolism ; RNA, Messenger - metabolism ; RNA-Binding Proteins - analysis ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins ; Sequence Homology, Amino Acid ; Staphylococcal Protein A - genetics ; transfer ; yeast ; Yeasts - genetics ; Yeasts - growth & development ; Yeasts - metabolism</subject><ispartof>The EMBO journal, 1997-08, Vol.16 (16), p.5086-5097</ispartof><rights>European Molecular Biology Organization 1997</rights><rights>Copyright © 1997 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170143/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170143/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9305650$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Teizeira, M.T</creatorcontrib><creatorcontrib>Siniossoglou, S</creatorcontrib><creatorcontrib>Podtelejnikov, S</creatorcontrib><creatorcontrib>Benichou, J.C</creatorcontrib><creatorcontrib>Mann, M</creatorcontrib><creatorcontrib>Dujon, B</creatorcontrib><creatorcontrib>Hurt, E</creatorcontrib><creatorcontrib>Fabre, E</creatorcontrib><title>Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Nup145p is an essential yeast nucleoporin involved in nuclear export of polyadenylated RNAs. We demonstrate here that Nup145p is cleaved
in vivo
to yield two functionally distinct domains: a carboxy‐terminal domain (C‐Nup145p) which is located at the nuclear pore complex (NPC) and assembles into the Nup84p complex, and a GLFG‐containing amino‐terminal domain (N‐Nup145p) which is not part of this complex. Whereas the essential C‐Nup145p accomplishes the functions required for efficient mRNA export and normal NPC distribution, N‐Nup145p, which is homologous to the GLFG‐containing nucleoporins Nup100p and Nup116p, is not necessary for cell growth. However, the N‐Nup145p becomes essential in a
nup188
mutant background. Strikingly, generation of a free N‐domain is a prerequisite for complementation of this peculiar synthetic lethal mutant. These data suggest that N‐ and C‐domains of Nup145p perform independent functions, and that the
in vivo
cleavage observed is of functional importance.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Biological Transport - physiology</subject><subject>Blotting, Western</subject><subject>cell membranes</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fungal Proteins - analysis</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>lethal mutants</subject><subject>messenger RNA</subject><subject>messenger rna export</subject><subject>Microscopy, Electron</subject><subject>Molecular Sequence Data</subject><subject>mRNA export</subject><subject>Mutagenesis, Site-Directed - genetics</subject><subject>mutants</subject><subject>Nuclear Envelope - chemistry</subject><subject>Nuclear Envelope - metabolism</subject><subject>nuclear membrane</subject><subject>nuclear pore complex</subject><subject>nuclear pore complex distribution</subject><subject>Nuclear Pore Complex Proteins</subject><subject>Nuclear Proteins - metabolism</subject><subject>nuclei</subject><subject>nucleoporin</subject><subject>protein cleavage</subject><subject>Protein Processing, Post-Translational</subject><subject>proteins</subject><subject>proteolysis</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>RNA, Fungal - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-Binding Proteins - analysis</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Sequence Homology, Amino Acid</subject><subject>Staphylococcal Protein A - genetics</subject><subject>transfer</subject><subject>yeast</subject><subject>Yeasts - genetics</subject><subject>Yeasts - growth & development</subject><subject>Yeasts - metabolism</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kV-L1DAUxYMo67j67ouYL9Dd_GnaxAdBl3VWWUfBWXwMSZt2M3aSkrQd--03Y5dBH4QLl8s5vxPIAeA1RhcYCXpp9trvLnFxkYYhXjwBK5wXKCOoZE_BCpECZznm4jl4EeMOIcR4ic_AmaCIFQytwGF78LAZXTVY71TXzbC2cbDphrXfK-sibI0zQQ2mhnqG1sHJTh5WnVGTag30DdyMPc5Z_w4q6PxkOqitP0LRRtir4f6gZtj4AN2YKN_7kFJfgmeN6qJ59bjPwd2n6-3VTXb7bf356sNt1uSYFZnRNdd5hbTCNcE5J4Q3ilBa0soQLagQWjHKGTKi0qauKmJMJaq6piqnmHJ6Dt4vuf2o98lg3BBUJ_tg9yrM0isr_1WcvZetnyTGJcI5TQFv_g44kY8_mHSx6AfbmfkkYySPBck_BUlcHOdYkLz--vFLyQTKeZFYvLAxYa41Qe78GFIN8b98YrKFSTWZ36f3VPgli5KWTP7crOX2-4auN1sk18n_dvE3ykvVBhvl3Q-CMEWEl4KRkj4AfLayCg</recordid><startdate>19970815</startdate><enddate>19970815</enddate><creator>Teizeira, M.T</creator><creator>Siniossoglou, S</creator><creator>Podtelejnikov, S</creator><creator>Benichou, J.C</creator><creator>Mann, M</creator><creator>Dujon, B</creator><creator>Hurt, E</creator><creator>Fabre, E</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>5PM</scope></search><sort><creationdate>19970815</creationdate><title>Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins</title><author>Teizeira, M.T ; Siniossoglou, S ; Podtelejnikov, S ; Benichou, J.C ; Mann, M ; Dujon, B ; Hurt, E ; Fabre, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f4156-ebd8b4c0ba1d2148228fa23373ce2b9399ba53850e9cbedcc2eec9cdd3a431383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Biological Transport - physiology</topic><topic>Blotting, Western</topic><topic>cell membranes</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fungal Proteins - analysis</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>lethal mutants</topic><topic>messenger RNA</topic><topic>messenger rna export</topic><topic>Microscopy, Electron</topic><topic>Molecular Sequence Data</topic><topic>mRNA export</topic><topic>Mutagenesis, Site-Directed - genetics</topic><topic>mutants</topic><topic>Nuclear Envelope - chemistry</topic><topic>Nuclear Envelope - metabolism</topic><topic>nuclear membrane</topic><topic>nuclear pore complex</topic><topic>nuclear pore complex distribution</topic><topic>Nuclear Pore Complex Proteins</topic><topic>Nuclear Proteins - metabolism</topic><topic>nuclei</topic><topic>nucleoporin</topic><topic>protein cleavage</topic><topic>Protein Processing, Post-Translational</topic><topic>proteins</topic><topic>proteolysis</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>RNA, Fungal - metabolism</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA-Binding Proteins - analysis</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Sequence Homology, Amino Acid</topic><topic>Staphylococcal Protein A - genetics</topic><topic>transfer</topic><topic>yeast</topic><topic>Yeasts - genetics</topic><topic>Yeasts - growth & development</topic><topic>Yeasts - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Teizeira, M.T</creatorcontrib><creatorcontrib>Siniossoglou, S</creatorcontrib><creatorcontrib>Podtelejnikov, S</creatorcontrib><creatorcontrib>Benichou, J.C</creatorcontrib><creatorcontrib>Mann, M</creatorcontrib><creatorcontrib>Dujon, B</creatorcontrib><creatorcontrib>Hurt, E</creatorcontrib><creatorcontrib>Fabre, E</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</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>Teizeira, M.T</au><au>Siniossoglou, S</au><au>Podtelejnikov, S</au><au>Benichou, J.C</au><au>Mann, M</au><au>Dujon, B</au><au>Hurt, E</au><au>Fabre, E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>1997-08-15</date><risdate>1997</risdate><volume>16</volume><issue>16</issue><spage>5086</spage><epage>5097</epage><pages>5086-5097</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><abstract>Nup145p is an essential yeast nucleoporin involved in nuclear export of polyadenylated RNAs. We demonstrate here that Nup145p is cleaved
in vivo
to yield two functionally distinct domains: a carboxy‐terminal domain (C‐Nup145p) which is located at the nuclear pore complex (NPC) and assembles into the Nup84p complex, and a GLFG‐containing amino‐terminal domain (N‐Nup145p) which is not part of this complex. Whereas the essential C‐Nup145p accomplishes the functions required for efficient mRNA export and normal NPC distribution, N‐Nup145p, which is homologous to the GLFG‐containing nucleoporins Nup100p and Nup116p, is not necessary for cell growth. However, the N‐Nup145p becomes essential in a
nup188
mutant background. Strikingly, generation of a free N‐domain is a prerequisite for complementation of this peculiar synthetic lethal mutant. These data suggest that N‐ and C‐domains of Nup145p perform independent functions, and that the
in vivo
cleavage observed is of functional importance.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>9305650</pmid><doi>10.1093/emboj/16.16.5086</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The EMBO journal, 1997-08, Vol.16 (16), p.5086-5097 |
| issn | 0261-4189 1460-2075 |
| language | eng |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence amino acid sequences Biological Transport - physiology Blotting, Western cell membranes Electrophoresis, Polyacrylamide Gel Fungal Proteins - analysis Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism lethal mutants messenger RNA messenger rna export Microscopy, Electron Molecular Sequence Data mRNA export Mutagenesis, Site-Directed - genetics mutants Nuclear Envelope - chemistry Nuclear Envelope - metabolism nuclear membrane nuclear pore complex nuclear pore complex distribution Nuclear Pore Complex Proteins Nuclear Proteins - metabolism nuclei nucleoporin protein cleavage Protein Processing, Post-Translational proteins proteolysis Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism RNA, Fungal - metabolism RNA, Messenger - metabolism RNA-Binding Proteins - analysis RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Staphylococcal Protein A - genetics transfer yeast Yeasts - genetics Yeasts - growth & development Yeasts - metabolism |
| title | Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins |
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