Glycosylation and processing of prepro-α-factor through the yeast secretory pathway
Identifieur interne : 000693 ( Istex/Corpus ); précédent : 000692; suivant : 000694Glycosylation and processing of prepro-α-factor through the yeast secretory pathway
Auteurs : David Julius ; Randy Schekman ; Jeremy ThornerSource :
- Cell [ 0092-8674 ] ; 1984.
English descriptors
- Teeft :
- Animal cells, Biol, Biosynthesis, Brake, Carbohydrate, Carbohydrate chains, Cell lysates, Centrifugation, Cerevisiae, Chem, Cleavage, Core oligosaccharides, Endo, Endoplasmic reticulum, Entire secretory pathway, Equal portions, Equal volume, Esmon, Experimental procedures, Field mata, Glycoprotein, Glycosyl chains, Glycosylated, Glycosylated form, Glycosylated precursor, Glycosylation, Golgi, Golgi apparatus, Granule, Immunoprecipitated, Invertase, Lysates, Mata, Mata cells, Mata secl8, Mature pheromone, Mature secretory granules, Microsome, Minimal medium, Molecular weight, Mutant, Mutation, Novick, Oligosaccharide, Oligosaccharide chains, Pancreas, Pancreas microsomes, Pathway, Peptide, Pheromone, Polypeptide, Precursor, Proteolytic, Proteolytic processing, Restrictive temperature, Saccharomyces, Saccharomyces cerevisiae, Same medium, Schekman, Secl, Secl8, Secl8 cells, Secretion, Secretory, Secretory granules, Secretory pathway, Secretory vesicles, Signal sequence, Thorner, Translation product, Tunicamycin, Tunicamycin treatment, Vesicle, Water bath, Wheat germ, Yeast, Yeast secretory pathway.
Abstract
Abstract: Events in the synthesis and processing of prepro-α-factor have been assessed with the aid of mutants blocked at various stages in the yeast secretory pathway. In normal cells treated with tunicamycin, a precursor accumulates which is identical in molecular weight to the primary translation product synthesized in vitro. At the restrictive temperature in a mutant blocked early in the pathway (sec53), a molecule of similar molecular weight accumulates. In mutants affecting translocation into (sec59) and passage from (sec18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed. The glycosylated precursor first experiences proteolytic processing when accumulated in a mutant (sec7) blocked at the stage of the Golgi apparatus. Substantially greater amounts of the mature pheromone are seen in mutants that accumulate secretory vesicles (sec1, sec2, sec3, sec5).
Url:
DOI: 10.1016/0092-8674(84)90224-1
Links to Exploration step
ISTEX:A51AA3F9D0779712D69A07B6CED82E83D75856B0Le document en format XML
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temperature</term><term>Saccharomyces</term><term>Saccharomyces cerevisiae</term><term>Same medium</term><term>Schekman</term><term>Secl</term><term>Secl8</term><term>Secl8 cells</term><term>Secretion</term><term>Secretory</term><term>Secretory granules</term><term>Secretory pathway</term><term>Secretory vesicles</term><term>Signal sequence</term><term>Thorner</term><term>Translation product</term><term>Tunicamycin</term><term>Tunicamycin treatment</term><term>Vesicle</term><term>Water bath</term><term>Wheat germ</term><term>Yeast</term><term>Yeast secretory pathway</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Events in the synthesis and processing of prepro-α-factor have been assessed with the aid of mutants blocked at various stages in the yeast secretory pathway. In normal cells treated with tunicamycin, a precursor accumulates which is identical in molecular weight to the primary translation product synthesized in vitro. At the restrictive temperature in a mutant blocked early in the pathway (sec53), a molecule of similar molecular weight accumulates. In mutants affecting translocation into (sec59) and passage from (sec18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed. The glycosylated precursor first experiences proteolytic processing when accumulated in a mutant (sec7) blocked at the stage of the Golgi apparatus. 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In normal cells treated with tunicamycin, a precursor accumulates which is identical in molecular weight to the primary translation product synthesized in vitro. At the restrictive temperature in a mutant blocked early in the pathway (sec53), a molecule of similar molecular weight accumulates. In mutants affecting translocation into (sec59) and passage from (sec18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed. The glycosylated precursor first experiences proteolytic processing when accumulated in a mutant (sec7) blocked at the stage of the Golgi apparatus. Substantially greater amounts of the mature pheromone are seen in mutants that accumulate secretory vesicles (sec1, sec2, sec3, sec5).</abstract><qualityIndicators><score>8.728</score><pdfWordCount>7317</pdfWordCount><pdfCharCount>47927</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>10</pdfPageCount><pdfPageSize>612.28 x 828 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>144</abstractWordCount><abstractCharCount>1005</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Glycosylation and processing of prepro-α-factor through the yeast secretory pathway</title><pmid><json:string>6420074</json:string></pmid><pii><json:string>0092-8674(84)90224-1</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Nat. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>80</volume><pages><first>7080</first><last>7084</last></pages></serie><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1984</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0513-2</json:string></pii><volume>36</volume><issue>2</issue><pages><first>309</first><last>318</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>36S</json:string><json:string>1984</json:string></date><geogName></geogName><orgName><json:string>Dormer Laboratory, Untversity of Calrfornra, Berkeley, California</json:string><json:string>Enzyme Center, Boston</json:string><json:string>Biochem</json:string><json:string>Yeast Genetic Stock Center</json:string><json:string>Sigma Chemical Co.</json:string><json:string>University of California</json:string><json:string>Department of Biochemistry University of California Berkeley, California</json:string><json:string>National Institute of General Medical Sciences</json:string></orgName><orgName_funder><json:string>National Institute of General Medical Sciences</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>J. Biol</json:string><json:string>B. E. Esmon</json:string><json:string>Hiroshi Nikaido</json:string><json:string>D. Shields</json:string><json:string>J. Thorner</json:string><json:string>J. Cell</json:string><json:string>A. Brake</json:string><json:string>Randy Schekman</json:string><json:string>J. Rubenstein</json:string><json:string>John Rubenstein</json:string><json:string>U.S.C. Section</json:string><json:string>Speed-Vat</json:string><json:string>Jeremy Nathans</json:string><json:string>I. Presence</json:string><json:string>Irene Schauer</json:string><json:string>Miles Biochemicals</json:string><json:string>Robert K. Mortimer</json:string><json:string>P. Robbins</json:string><json:string>C. Field</json:string><json:string>J. Nathans</json:string><json:string>L. Blair</json:string><json:string>Jeremy Thorner</json:string><json:string>D. Julius</json:string><json:string>Anthony Brake</json:string><json:string>Tom Stevens</json:string></persName><placeName><json:string>Hanover</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Ferro-Novick et al., 1984a</json:string><json:string>Novick et al., 1981</json:string><json:string>Singh et al., 1983</json:string><json:string>Yfactor respectively (for review see Thorner, 1981</json:string><json:string>Hanover et al., 1982</json:string><json:string>Emr et al., 1983</json:string><json:string>Gibson et al. (1982)</json:string><json:string>Novick et al., 1980</json:string><json:string>Gumbiner and Kelly, 1982</json:string><json:string>Machida and Kabat, 1982</json:string><json:string>Steiner, 1976</json:string><json:string>Huffaker and Robbins, 1982</json:string><json:string>Ferro-Novick et al. (1984a, 1984b)</json:string><json:string>Penman et al., 1982</json:string><json:string>Julius et al., 1983</json:string><json:string>Mollay et al., 1980</json:string><json:string>for review see Schekman, 1982</json:string><json:string>Carlson et al., 1983</json:string><json:string>Gumbiner and Kelly, 1981</json:string><json:string>Herbert and Uhler, 1982</json:string><json:string>Esmon et al., 1981</json:string><json:string>Prakash et al., 1983</json:string><json:string>Zhang et al., 1982</json:string><json:string>Fields et al., 1981</json:string><json:string>Perlman et al., 1982</json:string><json:string>Bostian et al., 1983</json:string><json:string>Y. Jones-Brown et al.</json:string><json:string>Kreil, 1973</json:string><json:string>Julius et al.. 1963</json:string><json:string>Cieiek and Thorner, 1979</json:string><json:string>Bussey et al., 1983</json:string><json:string>Sherman et al., 1979</json:string><json:string>Rubenstein and Chappell, 1983</json:string><json:string>Goldstern and Lampen, 1975</json:string><json:string>Brownstein et al., 1980</json:string><json:string>Tarentino et al., 1974</json:string><json:string>Laemmli, 1970</json:string><json:string>Kurjan and Herskowitz, 1982</json:string><json:string>Hasilik and Tanner, 1978</json:string><json:string>Ferro-Novick et al., 1984b</json:string><json:string>Robbins, 1982</json:string><json:string>Shields and Blobel, 1978</json:string><json:string>Neimann et al., 1982</json:string><json:string>Brake et al., 1983</json:string><json:string>Mahoney and Duskin, 1979</json:string><json:string>Julius et al., 1963</json:string><json:string>Blobel and Dobberstein, 1975</json:string><json:string>Ravazzola et al., 1983</json:string><json:string>Byrd et al., 1982</json:string><json:string>Struck et al., 1978</json:string><json:string>Esmon et al., 1961</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-N183QWFH-4</json:string></ark><categories><wos><json:string>1 - 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In normal cells treated with tunicamycin, a precursor accumulates which is identical in molecular weight to the primary translation product synthesized in vitro. At the restrictive temperature in a mutant blocked early in the pathway (sec53), a molecule of similar molecular weight accumulates. In mutants affecting translocation into (sec59) and passage from (sec18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed. The glycosylated precursor first experiences proteolytic processing when accumulated in a mutant (sec7) blocked at the stage of the Golgi apparatus. Substantially greater amounts of the mature pheromone are seen in mutants that accumulate secretory vesicles (sec1, sec2, sec3, sec5).</p></abstract></profileDesc><revisionDesc><change when="1983-12-01">Modified</change><change when="1984">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-N183QWFH-4/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>CELL</jid><aid>84902241</aid><ce:pii>0092-8674(84)90224-1</ce:pii><ce:doi>10.1016/0092-8674(84)90224-1</ce:doi><ce:copyright type="unknown" year="1984"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Glycosylation and processing of prepro-α-factor through the yeast secretory pathway</ce:title><ce:author-group><ce:author><ce:given-name>David</ce:given-name><ce:surname>Julius</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Randy</ce:given-name><ce:surname>Schekman</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jeremy</ce:given-name><ce:surname>Thorner</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Microbiology and Immunology University of California Berkeley, California 94720 USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Biochemistry University of California Berkeley, California 94720 USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="11" month="10" year="1983"></ce:date-received><ce:date-revised day="1" month="12" year="1983"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Events in the synthesis and processing of prepro-α-factor have been assessed with the aid of mutants blocked at various stages in the yeast secretory pathway. In normal cells treated with tunicamycin, a precursor accumulates which is identical in molecular weight to the primary translation product synthesized in vitro. At the restrictive temperature in a mutant blocked early in the pathway (sec53), a molecule of similar molecular weight accumulates. In mutants affecting translocation into (sec59) and passage from (sec18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed. The glycosylated precursor first experiences proteolytic processing when accumulated in a mutant (sec7) blocked at the stage of the Golgi apparatus. Substantially greater amounts of the mature pheromone are seen in mutants that accumulate secretory vesicles (sec1, sec2, sec3, sec5).</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Glycosylation and processing of prepro-α-factor through the yeast secretory pathway</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Glycosylation and processing of prepro-α-factor through the yeast secretory pathway</title></titleInfo><name type="personal"><namePart type="given">David</namePart><namePart type="family">Julius</namePart><affiliation>Department of Microbiology and Immunology University of California Berkeley, California 94720 USA</affiliation><affiliation>Department of Biochemistry University of California Berkeley, California 94720 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Randy</namePart><namePart type="family">Schekman</namePart><affiliation>Department of Biochemistry University of California Berkeley, California 94720 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jeremy</namePart><namePart type="family">Thorner</namePart><affiliation>Department of Microbiology and Immunology University of California Berkeley, California 94720 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1984</dateIssued><dateModified encoding="w3cdtf">1983-12-01</dateModified><copyrightDate encoding="w3cdtf">1984</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Events in the synthesis and processing of prepro-α-factor have been assessed with the aid of mutants blocked at various stages in the yeast secretory pathway. In normal cells treated with tunicamycin, a precursor accumulates which is identical in molecular weight to the primary translation product synthesized in vitro. At the restrictive temperature in a mutant blocked early in the pathway (sec53), a molecule of similar molecular weight accumulates. In mutants affecting translocation into (sec59) and passage from (sec18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed. The glycosylated precursor first experiences proteolytic processing when accumulated in a mutant (sec7) blocked at the stage of the Golgi apparatus. Substantially greater amounts of the mature pheromone are seen in mutants that accumulate secretory vesicles (sec1, sec2, sec3, sec5).</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1984</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0513-2</identifier><part><date>1984</date><detail type="volume"><number>36</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>235</start><end>566</end></extent><extent unit="pages"><start>309</start><end>318</end></extent></part></relatedItem><identifier type="istex">A51AA3F9D0779712D69A07B6CED82E83D75856B0</identifier><identifier type="ark">ark:/67375/6H6-N183QWFH-4</identifier><identifier type="DOI">10.1016/0092-8674(84)90224-1</identifier><identifier type="PII">0092-8674(84)90224-1</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-N183QWFH-4/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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