In vitro uptake and processing of prezein and other maize preproteins by maize membranes
A cell-free, mRNA-dependent system has been developed for the translation and processing of zein preproteins. A rough endoplasmic reticulum (RER)-enriched fraction, isolated by sucrose density gradients, can be treated with micrococcal nuclease to destroy endogenous messages. When these membranes ar...
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| Veröffentlicht in: | J. Cell Biol.; (United States) 1981-08, Vol.90 (2), p.427-434 |
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| creator | Burr, F. A. Burr, B. |
| description | A cell-free, mRNA-dependent system has been developed for the translation and processing of zein preproteins. A rough endoplasmic reticulum (RER)-enriched fraction, isolated by sucrose density gradients, can be treated with micrococcal nuclease to destroy endogenous messages. When these membranes are added to a wheat germ protein-synthesizing system together with zein mRNA, synthesis and processing of the polypeptides to the mature products takes place. The RER fraction from the endosperm has a different protein composition than that prepared from either the shoot or nucellar tissue and processes prezein more efficiently. The cleavage of the preproteins appears to be a cotranslational step as the completed preprotein chains cannot be processed, although they can be taken up to a limited extent. This small uptake, or absorption, of unprocessed zein seems to be an artifact and may be related to the unusual solubility properties of zein. Finally a sodium dodecyl sulfate (SDS)-urea polyacrylamide gel system has been developed which is particularly suited for the separation of low molecular weight proteins ( |
| doi_str_mv | 10.1083/jcb.90.2.427 |
| format | Article |
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A. ; Burr, B.</creator><creatorcontrib>Burr, F. A. ; Burr, B. ; Brookhaven National Lab., Upton, NY</creatorcontrib><description>A cell-free, mRNA-dependent system has been developed for the translation and processing of zein preproteins. A rough endoplasmic reticulum (RER)-enriched fraction, isolated by sucrose density gradients, can be treated with micrococcal nuclease to destroy endogenous messages. When these membranes are added to a wheat germ protein-synthesizing system together with zein mRNA, synthesis and processing of the polypeptides to the mature products takes place. The RER fraction from the endosperm has a different protein composition than that prepared from either the shoot or nucellar tissue and processes prezein more efficiently. The cleavage of the preproteins appears to be a cotranslational step as the completed preprotein chains cannot be processed, although they can be taken up to a limited extent. This small uptake, or absorption, of unprocessed zein seems to be an artifact and may be related to the unusual solubility properties of zein. Finally a sodium dodecyl sulfate (SDS)-urea polyacrylamide gel system has been developed which is particularly suited for the separation of low molecular weight proteins (<10,000 daltons). Using this method, we examined the products of in vitro zein processing and detected no presequence polypeptides. This suggests that the zein cleavage proteinase is probably an exopeptidase.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.90.2.427</identifier><identifier>PMID: 7026572</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>550200 - Biochemistry ; 553000 - Agriculture & Food Technology ; 60 APPLIED LIFE SCIENCES ; BASIC BIOLOGICAL SCIENCES ; BIOSYNTHESIS ; CELL CONSTITUENTS ; Cell free system ; CEREALS ; Corn ; ELECTROPHORESIS ; ENDOPLASMIC RETICULUM ; Endoplasmic Reticulum - metabolism ; Endosperm ; ENZYMES ; Exopeptidases ; Gels ; GRAMINEAE ; GRASS ; GROWTH ; IN VITRO ; MAIZE ; MEMBRANES ; MESSENGER-RNA ; Nuclear membrane ; NUCLEIC ACIDS ; ORGANIC COMPOUNDS ; ORGANOIDS ; P branes ; Peptide Hydrolases - metabolism ; PLANT GROWTH ; Plant Proteins - metabolism ; PLANTS ; Polyribosomes ; Protein Biosynthesis ; Protein Precursors - metabolism ; PROTEINS ; RNA ; RNA, Messenger - metabolism ; SYNTHESIS ; Zea mays - metabolism ; Zein - metabolism</subject><ispartof>J. Cell Biol.; (United States), 1981-08, Vol.90 (2), p.427-434</ispartof><rights>Copyright 1981 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3657-65371c8f5539f7ae1534993184d8e3ab5dacb6678395f3e569ce891e098fa1d43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7026572$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/5241982$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Burr, F. A.</creatorcontrib><creatorcontrib>Burr, B.</creatorcontrib><creatorcontrib>Brookhaven National Lab., Upton, NY</creatorcontrib><title>In vitro uptake and processing of prezein and other maize preproteins by maize membranes</title><title>J. Cell Biol.; (United States)</title><addtitle>J Cell Biol</addtitle><description>A cell-free, mRNA-dependent system has been developed for the translation and processing of zein preproteins. A rough endoplasmic reticulum (RER)-enriched fraction, isolated by sucrose density gradients, can be treated with micrococcal nuclease to destroy endogenous messages. When these membranes are added to a wheat germ protein-synthesizing system together with zein mRNA, synthesis and processing of the polypeptides to the mature products takes place. The RER fraction from the endosperm has a different protein composition than that prepared from either the shoot or nucellar tissue and processes prezein more efficiently. The cleavage of the preproteins appears to be a cotranslational step as the completed preprotein chains cannot be processed, although they can be taken up to a limited extent. This small uptake, or absorption, of unprocessed zein seems to be an artifact and may be related to the unusual solubility properties of zein. Finally a sodium dodecyl sulfate (SDS)-urea polyacrylamide gel system has been developed which is particularly suited for the separation of low molecular weight proteins (<10,000 daltons). Using this method, we examined the products of in vitro zein processing and detected no presequence polypeptides. This suggests that the zein cleavage proteinase is probably an exopeptidase.</description><subject>550200 - Biochemistry</subject><subject>553000 - Agriculture & Food Technology</subject><subject>60 APPLIED LIFE SCIENCES</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BIOSYNTHESIS</subject><subject>CELL CONSTITUENTS</subject><subject>Cell free system</subject><subject>CEREALS</subject><subject>Corn</subject><subject>ELECTROPHORESIS</subject><subject>ENDOPLASMIC RETICULUM</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Endosperm</subject><subject>ENZYMES</subject><subject>Exopeptidases</subject><subject>Gels</subject><subject>GRAMINEAE</subject><subject>GRASS</subject><subject>GROWTH</subject><subject>IN VITRO</subject><subject>MAIZE</subject><subject>MEMBRANES</subject><subject>MESSENGER-RNA</subject><subject>Nuclear membrane</subject><subject>NUCLEIC ACIDS</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANOIDS</subject><subject>P branes</subject><subject>Peptide Hydrolases - metabolism</subject><subject>PLANT GROWTH</subject><subject>Plant Proteins - metabolism</subject><subject>PLANTS</subject><subject>Polyribosomes</subject><subject>Protein Biosynthesis</subject><subject>Protein Precursors - metabolism</subject><subject>PROTEINS</subject><subject>RNA</subject><subject>RNA, Messenger - metabolism</subject><subject>SYNTHESIS</subject><subject>Zea mays - metabolism</subject><subject>Zein - metabolism</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkUtvEzEUhS0EKqGwYwlo1AUrJvg99gapqnhUqsQCKrGzPJ47iUPGDrZTqf31OExU2pV17_l0fK4OQq8JXhKs2MeN65caL-mS0-4JWhDBcasIx0_RAmNKWi2oeI5e5LzBGPOOsxN00mEqRUcX6NdlaG58SbHZ74r9DY0NQ7NL0UHOPqyaONYJ7sCHf0osa0jNZP0dHPYVLFXKTX97XE4w9ckGyC_Rs9FuM7w6vqfo-svnnxff2qvvXy8vzq9ax2qCVgrWEadGIZgeOwtEMK41I4oPCpjtxWBdL2WnmBYjAyG1A6UJYK1GSwbOTtGn2Xe37ycYHISS7Nbskp9sujXRevNYCX5tVvHGUEKIkrIanM0GMRdvsvMF3NrFEMAVIygnWtEKvT_-kuKfPeRiJp8dbLf11LjPpmNSEclxBT_MoEsx5wTjfRKCzaEuU-syGhtqal0Vf_sw_T187Kfqb2Z9k0tM_70k1lwdjn83y6ONxq6Sz-b6xyEw7qSsDuwv0Lmjzg</recordid><startdate>19810801</startdate><enddate>19810801</enddate><creator>Burr, F. A.</creator><creator>Burr, B.</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</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>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>19810801</creationdate><title>In vitro uptake and processing of prezein and other maize preproteins by maize membranes</title><author>Burr, F. A. ; Burr, B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3657-65371c8f5539f7ae1534993184d8e3ab5dacb6678395f3e569ce891e098fa1d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>550200 - Biochemistry</topic><topic>553000 - Agriculture & Food Technology</topic><topic>60 APPLIED LIFE SCIENCES</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BIOSYNTHESIS</topic><topic>CELL CONSTITUENTS</topic><topic>Cell free system</topic><topic>CEREALS</topic><topic>Corn</topic><topic>ELECTROPHORESIS</topic><topic>ENDOPLASMIC RETICULUM</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Endosperm</topic><topic>ENZYMES</topic><topic>Exopeptidases</topic><topic>Gels</topic><topic>GRAMINEAE</topic><topic>GRASS</topic><topic>GROWTH</topic><topic>IN VITRO</topic><topic>MAIZE</topic><topic>MEMBRANES</topic><topic>MESSENGER-RNA</topic><topic>Nuclear membrane</topic><topic>NUCLEIC ACIDS</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANOIDS</topic><topic>P branes</topic><topic>Peptide Hydrolases - metabolism</topic><topic>PLANT GROWTH</topic><topic>Plant Proteins - metabolism</topic><topic>PLANTS</topic><topic>Polyribosomes</topic><topic>Protein Biosynthesis</topic><topic>Protein Precursors - metabolism</topic><topic>PROTEINS</topic><topic>RNA</topic><topic>RNA, Messenger - metabolism</topic><topic>SYNTHESIS</topic><topic>Zea mays - metabolism</topic><topic>Zein - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Burr, F. A.</creatorcontrib><creatorcontrib>Burr, B.</creatorcontrib><creatorcontrib>Brookhaven National Lab., Upton, NY</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>J. Cell Biol.; (United States)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Burr, F. A.</au><au>Burr, B.</au><aucorp>Brookhaven National Lab., Upton, NY</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In vitro uptake and processing of prezein and other maize preproteins by maize membranes</atitle><jtitle>J. Cell Biol.; (United States)</jtitle><addtitle>J Cell Biol</addtitle><date>1981-08-01</date><risdate>1981</risdate><volume>90</volume><issue>2</issue><spage>427</spage><epage>434</epage><pages>427-434</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><abstract>A cell-free, mRNA-dependent system has been developed for the translation and processing of zein preproteins. A rough endoplasmic reticulum (RER)-enriched fraction, isolated by sucrose density gradients, can be treated with micrococcal nuclease to destroy endogenous messages. When these membranes are added to a wheat germ protein-synthesizing system together with zein mRNA, synthesis and processing of the polypeptides to the mature products takes place. The RER fraction from the endosperm has a different protein composition than that prepared from either the shoot or nucellar tissue and processes prezein more efficiently. The cleavage of the preproteins appears to be a cotranslational step as the completed preprotein chains cannot be processed, although they can be taken up to a limited extent. This small uptake, or absorption, of unprocessed zein seems to be an artifact and may be related to the unusual solubility properties of zein. Finally a sodium dodecyl sulfate (SDS)-urea polyacrylamide gel system has been developed which is particularly suited for the separation of low molecular weight proteins (<10,000 daltons). Using this method, we examined the products of in vitro zein processing and detected no presequence polypeptides. This suggests that the zein cleavage proteinase is probably an exopeptidase.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>7026572</pmid><doi>10.1083/jcb.90.2.427</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | J. Cell Biol.; (United States), 1981-08, Vol.90 (2), p.427-434 |
| issn | 0021-9525 1540-8140 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2111866 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | 550200 - Biochemistry 553000 - Agriculture & Food Technology 60 APPLIED LIFE SCIENCES BASIC BIOLOGICAL SCIENCES BIOSYNTHESIS CELL CONSTITUENTS Cell free system CEREALS Corn ELECTROPHORESIS ENDOPLASMIC RETICULUM Endoplasmic Reticulum - metabolism Endosperm ENZYMES Exopeptidases Gels GRAMINEAE GRASS GROWTH IN VITRO MAIZE MEMBRANES MESSENGER-RNA Nuclear membrane NUCLEIC ACIDS ORGANIC COMPOUNDS ORGANOIDS P branes Peptide Hydrolases - metabolism PLANT GROWTH Plant Proteins - metabolism PLANTS Polyribosomes Protein Biosynthesis Protein Precursors - metabolism PROTEINS RNA RNA, Messenger - metabolism SYNTHESIS Zea mays - metabolism Zein - metabolism |
| title | In vitro uptake and processing of prezein and other maize preproteins by maize membranes |
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