A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane
The maize (Zea mays L.) floury-2 (fl2) mutation is associated with a general decrease in storage protein synthesis, altered protein body morphology, and the synthesis of a novel 24-kD alpha-zein storage protein. Unlike storage proteins in normal kernels and the majority of storage proteins in fl2 ke...
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| Veröffentlicht in: | Plant Physiology (Bethesda) 1997-05, Vol.114 (1), p.345-352 |
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| creator | Gillikin, J.W. (North Carolina State University, Raleigh, NC.) Zhang, F Coleman, C.E Bass, H.W Larkins, B.A Boston, R.S |
| description | The maize (Zea mays L.) floury-2 (fl2) mutation is associated with a general decrease in storage protein synthesis, altered protein body morphology, and the synthesis of a novel 24-kD alpha-zein storage protein. Unlike storage proteins in normal kernels and the majority of storage proteins in fl2 kernels, the 24-kD alpha-zein contains a signal peptide that would normally be removed during protein synthesis and processing. The expected processing site of this alpha-zein reveals a putative mutation alanine leads to valine (Ala leads to Val) that is not found at other junctions between signal sequences and mature proteins. To investigate the impact of such a mutation on signal peptide cleavage, we have assayed the 24-kD fl2 alpha-zein in a co-translational processing system in vitro. Translation of RNA from fl2 kernels or synthetic RNA encoding the fl2 alpha-zein in the presence of microsomes yielded a 24-kD polypeptide. A normal signal peptide sequence, generated by site-directed mutagenesis, restored the capacity of the RNA to direct synthesis of a properly processed protein in a cell-free system. Both the fl2 alpha-zein and the fl2 alpha-zein (Val leads to Ala) were translocated into the lumen of the endoplasmic reticulum. The processed fl2 alpha-zein (Val leads to Ala) was localized in the soluble portion of the microsomes, whereas the fl2 alpha-zein co-fractionated with the microsomal membranes. By remaining anchored to protein body membranes during endosperm maturation, the fl2 zein may thus constrain storage protein packing and perturb protein body morphology |
| doi_str_mv | 10.1104/pp.114.1.345 |
| format | Article |
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(North Carolina State University, Raleigh, NC.) ; Zhang, F ; Coleman, C.E ; Bass, H.W ; Larkins, B.A ; Boston, R.S</creator><creatorcontrib>Gillikin, J.W. (North Carolina State University, Raleigh, NC.) ; Zhang, F ; Coleman, C.E ; Bass, H.W ; Larkins, B.A ; Boston, R.S</creatorcontrib><description>The maize (Zea mays L.) floury-2 (fl2) mutation is associated with a general decrease in storage protein synthesis, altered protein body morphology, and the synthesis of a novel 24-kD alpha-zein storage protein. Unlike storage proteins in normal kernels and the majority of storage proteins in fl2 kernels, the 24-kD alpha-zein contains a signal peptide that would normally be removed during protein synthesis and processing. The expected processing site of this alpha-zein reveals a putative mutation alanine leads to valine (Ala leads to Val) that is not found at other junctions between signal sequences and mature proteins. To investigate the impact of such a mutation on signal peptide cleavage, we have assayed the 24-kD fl2 alpha-zein in a co-translational processing system in vitro. Translation of RNA from fl2 kernels or synthetic RNA encoding the fl2 alpha-zein in the presence of microsomes yielded a 24-kD polypeptide. A normal signal peptide sequence, generated by site-directed mutagenesis, restored the capacity of the RNA to direct synthesis of a properly processed protein in a cell-free system. Both the fl2 alpha-zein and the fl2 alpha-zein (Val leads to Ala) were translocated into the lumen of the endoplasmic reticulum. The processed fl2 alpha-zein (Val leads to Ala) was localized in the soluble portion of the microsomes, whereas the fl2 alpha-zein co-fractionated with the microsomal membranes. By remaining anchored to protein body membranes during endosperm maturation, the fl2 zein may thus constrain storage protein packing and perturb protein body morphology</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.114.1.345</identifier><identifier>PMID: 9159955</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>Amino acids ; Animals ; ARN ; Base Sequence ; BINDING PROTEINS ; BIOCHEMISTRY ; Biological and medical sciences ; BIOLOGY AND MEDICINE, BASIC STUDIES ; BIOSYNTHESIS ; Canines ; Cell Biology and Signal Transduction ; CLONACION ; CLONAGE ; CLONING ; Cloning, Molecular ; Corn ; CYTOPLASMIC ORGANELLES ; ENDOPLASMIC RETICULUM ; Endoplasmic Reticulum - metabolism ; Endosperm ; Fundamental and applied biological sciences. Psychology ; Gels ; Genetic mutation ; GENETIC REGULATION ; GENETIC VARIATION ; GENETICA ; GENETICS ; GENETIQUE ; In Vitro Techniques ; Intracellular Membranes - metabolism ; MAIZE ; Metabolism ; METABOLISME DES PROTEINES ; METABOLISMO PROTEICO ; MICROSOMES ; Microsomes - metabolism ; Models, Biological ; Molecular Sequence Data ; MUTACION ; MUTAGENESIS ; Mutagenesis, Site-Directed ; MUTANT ; MUTANTES ; MUTANTS ; MUTATION ; MUTATIONS ; Nitrogen metabolism ; Oligodeoxyribonucleotides - genetics ; ORGANITE CELLULAIRE ; ORGANULOS CITOPLASMICOS ; Phenotype ; Plant physiology and development ; Point Mutation ; PROLAMINAS ; PROLAMINE ; PROLAMINES ; Protein Biosynthesis ; PROTEIN METABOLISM ; Protein Sorting Signals - chemistry ; Protein Sorting Signals - genetics ; Protein Sorting Signals - metabolism ; PROTEIN SYNTHESIS ; PROTEIN TRANSPORT ; PROTEINAS AGLUTINANTES ; PROTEINE DE LIAISON ; PROTEINS ; Rabbits ; RETICULO ENDOPLASMATICO ; RETICULUM ENDOPLASMIQUE ; RNA ; Signal encoding ; SINTESIS DE PROTEINAS ; Storage proteins ; SYNTHESE PROTEIQUE ; TRANSCRIPCION ; TRANSCRIPTION ; TRANSLATION ; VARIACION GENETICA ; VARIATION GENETIQUE ; ZEA MAYS ; Zea mays - genetics ; Zea mays - metabolism ; Zein - chemistry ; Zein - genetics ; Zein - metabolism</subject><ispartof>Plant Physiology (Bethesda), 1997-05, Vol.114 (1), p.345-352</ispartof><rights>Copyright 1997 American Society of Plant Physiologists</rights><rights>1997 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c578t-bee8083d690f40d3f9a7bd31331296d6c941bfad641de993639a479e21faea263</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4277711$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4277711$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,778,782,801,883,27907,27908,58000,58233</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2775137$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9159955$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/530493$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Gillikin, J.W. (North Carolina State University, Raleigh, NC.)</creatorcontrib><creatorcontrib>Zhang, F</creatorcontrib><creatorcontrib>Coleman, C.E</creatorcontrib><creatorcontrib>Bass, H.W</creatorcontrib><creatorcontrib>Larkins, B.A</creatorcontrib><creatorcontrib>Boston, R.S</creatorcontrib><title>A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane</title><title>Plant Physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>The maize (Zea mays L.) floury-2 (fl2) mutation is associated with a general decrease in storage protein synthesis, altered protein body morphology, and the synthesis of a novel 24-kD alpha-zein storage protein. Unlike storage proteins in normal kernels and the majority of storage proteins in fl2 kernels, the 24-kD alpha-zein contains a signal peptide that would normally be removed during protein synthesis and processing. The expected processing site of this alpha-zein reveals a putative mutation alanine leads to valine (Ala leads to Val) that is not found at other junctions between signal sequences and mature proteins. To investigate the impact of such a mutation on signal peptide cleavage, we have assayed the 24-kD fl2 alpha-zein in a co-translational processing system in vitro. Translation of RNA from fl2 kernels or synthetic RNA encoding the fl2 alpha-zein in the presence of microsomes yielded a 24-kD polypeptide. A normal signal peptide sequence, generated by site-directed mutagenesis, restored the capacity of the RNA to direct synthesis of a properly processed protein in a cell-free system. Both the fl2 alpha-zein and the fl2 alpha-zein (Val leads to Ala) were translocated into the lumen of the endoplasmic reticulum. The processed fl2 alpha-zein (Val leads to Ala) was localized in the soluble portion of the microsomes, whereas the fl2 alpha-zein co-fractionated with the microsomal membranes. By remaining anchored to protein body membranes during endosperm maturation, the fl2 zein may thus constrain storage protein packing and perturb protein body morphology</description><subject>Amino acids</subject><subject>Animals</subject><subject>ARN</subject><subject>Base Sequence</subject><subject>BINDING PROTEINS</subject><subject>BIOCHEMISTRY</subject><subject>Biological and medical sciences</subject><subject>BIOLOGY AND MEDICINE, BASIC STUDIES</subject><subject>BIOSYNTHESIS</subject><subject>Canines</subject><subject>Cell Biology and Signal Transduction</subject><subject>CLONACION</subject><subject>CLONAGE</subject><subject>CLONING</subject><subject>Cloning, Molecular</subject><subject>Corn</subject><subject>CYTOPLASMIC ORGANELLES</subject><subject>ENDOPLASMIC RETICULUM</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Endosperm</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Genetic mutation</subject><subject>GENETIC REGULATION</subject><subject>GENETIC VARIATION</subject><subject>GENETICA</subject><subject>GENETICS</subject><subject>GENETIQUE</subject><subject>In Vitro Techniques</subject><subject>Intracellular Membranes - metabolism</subject><subject>MAIZE</subject><subject>Metabolism</subject><subject>METABOLISME DES PROTEINES</subject><subject>METABOLISMO PROTEICO</subject><subject>MICROSOMES</subject><subject>Microsomes - metabolism</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>MUTACION</subject><subject>MUTAGENESIS</subject><subject>Mutagenesis, Site-Directed</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>MUTANTS</subject><subject>MUTATION</subject><subject>MUTATIONS</subject><subject>Nitrogen metabolism</subject><subject>Oligodeoxyribonucleotides - genetics</subject><subject>ORGANITE CELLULAIRE</subject><subject>ORGANULOS CITOPLASMICOS</subject><subject>Phenotype</subject><subject>Plant physiology and development</subject><subject>Point Mutation</subject><subject>PROLAMINAS</subject><subject>PROLAMINE</subject><subject>PROLAMINES</subject><subject>Protein Biosynthesis</subject><subject>PROTEIN METABOLISM</subject><subject>Protein Sorting Signals - chemistry</subject><subject>Protein Sorting Signals - genetics</subject><subject>Protein Sorting Signals - metabolism</subject><subject>PROTEIN SYNTHESIS</subject><subject>PROTEIN TRANSPORT</subject><subject>PROTEINAS AGLUTINANTES</subject><subject>PROTEINE DE LIAISON</subject><subject>PROTEINS</subject><subject>Rabbits</subject><subject>RETICULO ENDOPLASMATICO</subject><subject>RETICULUM ENDOPLASMIQUE</subject><subject>RNA</subject><subject>Signal encoding</subject><subject>SINTESIS DE PROTEINAS</subject><subject>Storage proteins</subject><subject>SYNTHESE PROTEIQUE</subject><subject>TRANSCRIPCION</subject><subject>TRANSCRIPTION</subject><subject>TRANSLATION</subject><subject>VARIACION GENETICA</subject><subject>VARIATION GENETIQUE</subject><subject>ZEA MAYS</subject><subject>Zea mays - genetics</subject><subject>Zea mays - metabolism</subject><subject>Zein - chemistry</subject><subject>Zein - genetics</subject><subject>Zein - metabolism</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkcFvFCEUxonR1G315lETTDy6K2-AmeHQQ9NYNWniQXvxQhh47NLMDBNgm9S_XnQ3q174CN_vPV6-R8grYBsAJj4sS1WxgQ0X8glZgeTNupGif0pWjNU763v1nJznfM8YAw7ijJwpkEpJuSI_rqhDj7aEB6Q5bGcz0gWXEhzSgmWHKdN6Uj_GfXpcN_QnhpmW-OcRZxeX0eQpWJqwBLsf9xOdcBqSmfEFeebNmPHlUS_I3c3H79ef17dfP325vrpdW9n1ZT0g9qznrlXMC-a4V6YbHAfOoVGta60SMHjjWgEOleItV0Z0ChvwBk3T8gtyeei77IcJncW5JDPqJYXJpEcdTdD_O3PY6W180CB7DqzWvz3Ux1yCzjYUtDsb57mmoiVnQvHKvD8wNsWcE_pTe2D69xb0slQVGnTdQsXf_DvSCT7GXv13R99ka0Zf47Ihn7Cm6yTwrmKvD9h9LjGdbFH9DuDvL95Ebbapdrj7Bkp1dWTRtfwXIKGjWg</recordid><startdate>19970501</startdate><enddate>19970501</enddate><creator>Gillikin, J.W. (North Carolina State University, Raleigh, NC.)</creator><creator>Zhang, F</creator><creator>Coleman, C.E</creator><creator>Bass, H.W</creator><creator>Larkins, B.A</creator><creator>Boston, R.S</creator><general>American Society of Plant Physiologists</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>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>19970501</creationdate><title>A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane</title><author>Gillikin, J.W. (North Carolina State University, Raleigh, NC.) ; Zhang, F ; Coleman, C.E ; Bass, H.W ; Larkins, B.A ; Boston, R.S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c578t-bee8083d690f40d3f9a7bd31331296d6c941bfad641de993639a479e21faea263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>ARN</topic><topic>Base Sequence</topic><topic>BINDING PROTEINS</topic><topic>BIOCHEMISTRY</topic><topic>Biological and medical sciences</topic><topic>BIOLOGY AND MEDICINE, BASIC STUDIES</topic><topic>BIOSYNTHESIS</topic><topic>Canines</topic><topic>Cell Biology and Signal Transduction</topic><topic>CLONACION</topic><topic>CLONAGE</topic><topic>CLONING</topic><topic>Cloning, Molecular</topic><topic>Corn</topic><topic>CYTOPLASMIC ORGANELLES</topic><topic>ENDOPLASMIC RETICULUM</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Endosperm</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Genetic mutation</topic><topic>GENETIC REGULATION</topic><topic>GENETIC VARIATION</topic><topic>GENETICA</topic><topic>GENETICS</topic><topic>GENETIQUE</topic><topic>In Vitro Techniques</topic><topic>Intracellular Membranes - metabolism</topic><topic>MAIZE</topic><topic>Metabolism</topic><topic>METABOLISME DES PROTEINES</topic><topic>METABOLISMO PROTEICO</topic><topic>MICROSOMES</topic><topic>Microsomes - metabolism</topic><topic>Models, Biological</topic><topic>Molecular Sequence Data</topic><topic>MUTACION</topic><topic>MUTAGENESIS</topic><topic>Mutagenesis, Site-Directed</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>MUTANTS</topic><topic>MUTATION</topic><topic>MUTATIONS</topic><topic>Nitrogen metabolism</topic><topic>Oligodeoxyribonucleotides - genetics</topic><topic>ORGANITE CELLULAIRE</topic><topic>ORGANULOS CITOPLASMICOS</topic><topic>Phenotype</topic><topic>Plant physiology and development</topic><topic>Point Mutation</topic><topic>PROLAMINAS</topic><topic>PROLAMINE</topic><topic>PROLAMINES</topic><topic>Protein Biosynthesis</topic><topic>PROTEIN METABOLISM</topic><topic>Protein Sorting Signals - chemistry</topic><topic>Protein Sorting Signals - genetics</topic><topic>Protein Sorting Signals - metabolism</topic><topic>PROTEIN SYNTHESIS</topic><topic>PROTEIN TRANSPORT</topic><topic>PROTEINAS AGLUTINANTES</topic><topic>PROTEINE DE LIAISON</topic><topic>PROTEINS</topic><topic>Rabbits</topic><topic>RETICULO ENDOPLASMATICO</topic><topic>RETICULUM ENDOPLASMIQUE</topic><topic>RNA</topic><topic>Signal encoding</topic><topic>SINTESIS DE PROTEINAS</topic><topic>Storage proteins</topic><topic>SYNTHESE PROTEIQUE</topic><topic>TRANSCRIPCION</topic><topic>TRANSCRIPTION</topic><topic>TRANSLATION</topic><topic>VARIACION GENETICA</topic><topic>VARIATION GENETIQUE</topic><topic>ZEA MAYS</topic><topic>Zea mays - genetics</topic><topic>Zea mays - metabolism</topic><topic>Zein - chemistry</topic><topic>Zein - genetics</topic><topic>Zein - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gillikin, J.W. (North Carolina State University, Raleigh, NC.)</creatorcontrib><creatorcontrib>Zhang, F</creatorcontrib><creatorcontrib>Coleman, C.E</creatorcontrib><creatorcontrib>Bass, H.W</creatorcontrib><creatorcontrib>Larkins, B.A</creatorcontrib><creatorcontrib>Boston, R.S</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>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant Physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gillikin, J.W. (North Carolina State University, Raleigh, NC.)</au><au>Zhang, F</au><au>Coleman, C.E</au><au>Bass, H.W</au><au>Larkins, B.A</au><au>Boston, R.S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane</atitle><jtitle>Plant Physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1997-05-01</date><risdate>1997</risdate><volume>114</volume><issue>1</issue><spage>345</spage><epage>352</epage><pages>345-352</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>The maize (Zea mays L.) floury-2 (fl2) mutation is associated with a general decrease in storage protein synthesis, altered protein body morphology, and the synthesis of a novel 24-kD alpha-zein storage protein. Unlike storage proteins in normal kernels and the majority of storage proteins in fl2 kernels, the 24-kD alpha-zein contains a signal peptide that would normally be removed during protein synthesis and processing. The expected processing site of this alpha-zein reveals a putative mutation alanine leads to valine (Ala leads to Val) that is not found at other junctions between signal sequences and mature proteins. To investigate the impact of such a mutation on signal peptide cleavage, we have assayed the 24-kD fl2 alpha-zein in a co-translational processing system in vitro. Translation of RNA from fl2 kernels or synthetic RNA encoding the fl2 alpha-zein in the presence of microsomes yielded a 24-kD polypeptide. A normal signal peptide sequence, generated by site-directed mutagenesis, restored the capacity of the RNA to direct synthesis of a properly processed protein in a cell-free system. Both the fl2 alpha-zein and the fl2 alpha-zein (Val leads to Ala) were translocated into the lumen of the endoplasmic reticulum. The processed fl2 alpha-zein (Val leads to Ala) was localized in the soluble portion of the microsomes, whereas the fl2 alpha-zein co-fractionated with the microsomal membranes. By remaining anchored to protein body membranes during endosperm maturation, the fl2 zein may thus constrain storage protein packing and perturb protein body morphology</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>9159955</pmid><doi>10.1104/pp.114.1.345</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0032-0889 |
| ispartof | Plant Physiology (Bethesda), 1997-05, Vol.114 (1), p.345-352 |
| issn | 0032-0889 1532-2548 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_158310 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current) |
| subjects | Amino acids Animals ARN Base Sequence BINDING PROTEINS BIOCHEMISTRY Biological and medical sciences BIOLOGY AND MEDICINE, BASIC STUDIES BIOSYNTHESIS Canines Cell Biology and Signal Transduction CLONACION CLONAGE CLONING Cloning, Molecular Corn CYTOPLASMIC ORGANELLES ENDOPLASMIC RETICULUM Endoplasmic Reticulum - metabolism Endosperm Fundamental and applied biological sciences. Psychology Gels Genetic mutation GENETIC REGULATION GENETIC VARIATION GENETICA GENETICS GENETIQUE In Vitro Techniques Intracellular Membranes - metabolism MAIZE Metabolism METABOLISME DES PROTEINES METABOLISMO PROTEICO MICROSOMES Microsomes - metabolism Models, Biological Molecular Sequence Data MUTACION MUTAGENESIS Mutagenesis, Site-Directed MUTANT MUTANTES MUTANTS MUTATION MUTATIONS Nitrogen metabolism Oligodeoxyribonucleotides - genetics ORGANITE CELLULAIRE ORGANULOS CITOPLASMICOS Phenotype Plant physiology and development Point Mutation PROLAMINAS PROLAMINE PROLAMINES Protein Biosynthesis PROTEIN METABOLISM Protein Sorting Signals - chemistry Protein Sorting Signals - genetics Protein Sorting Signals - metabolism PROTEIN SYNTHESIS PROTEIN TRANSPORT PROTEINAS AGLUTINANTES PROTEINE DE LIAISON PROTEINS Rabbits RETICULO ENDOPLASMATICO RETICULUM ENDOPLASMIQUE RNA Signal encoding SINTESIS DE PROTEINAS Storage proteins SYNTHESE PROTEIQUE TRANSCRIPCION TRANSCRIPTION TRANSLATION VARIACION GENETICA VARIATION GENETIQUE ZEA MAYS Zea mays - genetics Zea mays - metabolism Zein - chemistry Zein - genetics Zein - metabolism |
| title | A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane |
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