Proteomic analysis of preharvest sprouting in rye using two-dimensional electrophoresis and mass spectrometry
Qualitative and quantitative differences were found between two-dimensional electrophoretic spectra of 546 proteins from two bulked samples of mature rye grain representing: (1) 20 recombinant inbred lines extremely resistant to preharvest sprouting and (2) 20 recombinant inbred lines extremely susc...
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| Veröffentlicht in: | Molecular breeding 2012-10, Vol.30 (3), p.1355-1361 |
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| description | Qualitative and quantitative differences were found between two-dimensional electrophoretic spectra of 546 proteins from two bulked samples of mature rye grain representing: (1) 20 recombinant inbred lines extremely resistant to preharvest sprouting and (2) 20 recombinant inbred lines extremely susceptible to preharvest sprouting. Mass spectrometry of resolved proteins showed that four spots specific for PHS susceptibility represented high molecular weight glutenin subunit, glutathione transferase, 16.9 kDa heat-shock protein, and monomeric alpha-amylase inhibitor. Two spots specific for PHS resistance contained cytosolic malate dehydrogenase and functionally unrecognized protein with sequence homology to rubber elongation factor protein. Majority of 14 proteins with at least two-fold higher accumulation level in preharvest sprouting susceptible lines relative to that found in sprouting resistant lines, showed sequence homology to proteins involved in defense mechanisms against biotic and abiotic stresses including oxidative stress, and those taking part in energy supply. Two spots were identified as regulatory proteins from the 14-3-3 family with one molecular form prevailing in sprouting susceptible and another form highly accumulated in sprouting resistant lines. Further study establishing map positions of the revealed structural genes in respect to quantitative trait loci for preharvest sprouting in rye should answer the question on their possible status as candidate genes. |
| doi_str_mv | 10.1007/s11032-012-9721-z |
| format | Article |
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Mass spectrometry of resolved proteins showed that four spots specific for PHS susceptibility represented high molecular weight glutenin subunit, glutathione transferase, 16.9 kDa heat-shock protein, and monomeric alpha-amylase inhibitor. Two spots specific for PHS resistance contained cytosolic malate dehydrogenase and functionally unrecognized protein with sequence homology to rubber elongation factor protein. Majority of 14 proteins with at least two-fold higher accumulation level in preharvest sprouting susceptible lines relative to that found in sprouting resistant lines, showed sequence homology to proteins involved in defense mechanisms against biotic and abiotic stresses including oxidative stress, and those taking part in energy supply. Two spots were identified as regulatory proteins from the 14-3-3 family with one molecular form prevailing in sprouting susceptible and another form highly accumulated in sprouting resistant lines. Further study establishing map positions of the revealed structural genes in respect to quantitative trait loci for preharvest sprouting in rye should answer the question on their possible status as candidate genes.</description><identifier>ISSN: 1380-3743</identifier><identifier>EISSN: 1572-9788</identifier><identifier>DOI: 10.1007/s11032-012-9721-z</identifier><identifier>PMID: 23024596</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>14-3-3 protein ; alpha-amylase ; Amino acid sequence ; Biomedical and Life Sciences ; Biotechnology ; defense mechanisms ; Electrophoresis ; Elongation ; Gene mapping ; Genes ; Glutathione ; Glutathione transferase ; Glutenin ; Heat shock proteins ; Homology ; inbred lines ; Inbreeding ; Life Sciences ; Malate dehydrogenase ; Mass spectrometry ; Mass spectroscopy ; Molecular biology ; Molecular weight ; Oxidative stress ; Plant biology ; Plant Genetics and Genomics ; Plant Pathology ; Plant Physiology ; Plant Sciences ; Protein folding ; Proteins ; proteomics ; Quantitative trait loci ; Regulatory proteins ; Rubber ; Rye ; Scientific imaging ; sequence homology ; Spectroscopy ; sprouting ; structural genes ; α-Amylase</subject><ispartof>Molecular breeding, 2012-10, Vol.30 (3), p.1355-1361</ispartof><rights>The Author(s) 2012</rights><rights>Molecular Breeding is a copyright of Springer, (2012). All Rights Reserved. © 2012. This work is published under https://creativecommons.org/licenses/by/2.0 (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c527t-97b93671e72197fa447b41c4129d40c8f9f35ba8d4e91475168b186375704b9d3</citedby><cites>FETCH-LOGICAL-c527t-97b93671e72197fa447b41c4129d40c8f9f35ba8d4e91475168b186375704b9d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11032-012-9721-z$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11032-012-9721-z$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23024596$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Masojć, Piotr</creatorcontrib><creatorcontrib>Kosmala, Arkadiusz</creatorcontrib><title>Proteomic analysis of preharvest sprouting in rye using two-dimensional electrophoresis and mass spectrometry</title><title>Molecular breeding</title><addtitle>Mol Breeding</addtitle><addtitle>Mol Breed</addtitle><description>Qualitative and quantitative differences were found between two-dimensional electrophoretic spectra of 546 proteins from two bulked samples of mature rye grain representing: (1) 20 recombinant inbred lines extremely resistant to preharvest sprouting and (2) 20 recombinant inbred lines extremely susceptible to preharvest sprouting. Mass spectrometry of resolved proteins showed that four spots specific for PHS susceptibility represented high molecular weight glutenin subunit, glutathione transferase, 16.9 kDa heat-shock protein, and monomeric alpha-amylase inhibitor. Two spots specific for PHS resistance contained cytosolic malate dehydrogenase and functionally unrecognized protein with sequence homology to rubber elongation factor protein. Majority of 14 proteins with at least two-fold higher accumulation level in preharvest sprouting susceptible lines relative to that found in sprouting resistant lines, showed sequence homology to proteins involved in defense mechanisms against biotic and abiotic stresses including oxidative stress, and those taking part in energy supply. Two spots were identified as regulatory proteins from the 14-3-3 family with one molecular form prevailing in sprouting susceptible and another form highly accumulated in sprouting resistant lines. Further study establishing map positions of the revealed structural genes in respect to quantitative trait loci for preharvest sprouting in rye should answer the question on their possible status as candidate genes.</description><subject>14-3-3 protein</subject><subject>alpha-amylase</subject><subject>Amino acid sequence</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>defense mechanisms</subject><subject>Electrophoresis</subject><subject>Elongation</subject><subject>Gene mapping</subject><subject>Genes</subject><subject>Glutathione</subject><subject>Glutathione transferase</subject><subject>Glutenin</subject><subject>Heat shock proteins</subject><subject>Homology</subject><subject>inbred lines</subject><subject>Inbreeding</subject><subject>Life Sciences</subject><subject>Malate dehydrogenase</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Molecular biology</subject><subject>Molecular weight</subject><subject>Oxidative stress</subject><subject>Plant biology</subject><subject>Plant Genetics and Genomics</subject><subject>Plant Pathology</subject><subject>Plant Physiology</subject><subject>Plant Sciences</subject><subject>Protein folding</subject><subject>Proteins</subject><subject>proteomics</subject><subject>Quantitative trait loci</subject><subject>Regulatory proteins</subject><subject>Rubber</subject><subject>Rye</subject><subject>Scientific imaging</subject><subject>sequence homology</subject><subject>Spectroscopy</subject><subject>sprouting</subject><subject>structural genes</subject><subject>α-Amylase</subject><issn>1380-3743</issn><issn>1572-9788</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFUk1v1TAQtBCIlsIP4AKWuHAJeP3tCxKqoEWqBBL0bDmJ856rJA52UvT663FIKR8HONmrnRnvzhihp0BeASHqdQYgjFYEaGUUhermHjoGodZK6_vlzjSpmOLsCD3K-YoUjpHyITqijFAujDxGw6cUZx-H0GA3uv6QQ8axw1Pye5eufZ5xnlJc5jDucBhxOni85LWYv8WqDYMfc4iFiH3vmznFaR-TX0Xc2OLB5Vz4PxqDn9PhMXrQuT77J7fnCbp8_-7L6Xl18fHsw-nbi6oRVM1l_NowqcCXpYzqHOeq5tBwoKblpNGd6ZionW65N8CVAKlr0JIpoQivTctO0JtNd1rqwbeNH-fkejulMLh0sNEF-2dnDHu7i9eWcUlAsSLw8lYgxa9LscEOITe-793o45ItaCqL0ZrJ_0MFM5xLKVboi7-gV3FJxb1sKRVGEKU4LyjYUE2KOSff3c0NxK652y13W3K3a-72pnCe_b7wHeNn0AVAN0CJs8Tn06-n_6X6fCN1Llq3SyHby8-UAC8_SUoQhH0HOCDD0g</recordid><startdate>20121001</startdate><enddate>20121001</enddate><creator>Masojć, Piotr</creator><creator>Kosmala, Arkadiusz</creator><general>Springer-Verlag</general><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>C6C</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X2</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M0K</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7S9</scope><scope>L.6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20121001</creationdate><title>Proteomic analysis of preharvest sprouting in rye using two-dimensional electrophoresis and mass spectrometry</title><author>Masojć, Piotr ; Kosmala, Arkadiusz</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c527t-97b93671e72197fa447b41c4129d40c8f9f35ba8d4e91475168b186375704b9d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>14-3-3 protein</topic><topic>alpha-amylase</topic><topic>Amino acid sequence</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>defense mechanisms</topic><topic>Electrophoresis</topic><topic>Elongation</topic><topic>Gene mapping</topic><topic>Genes</topic><topic>Glutathione</topic><topic>Glutathione transferase</topic><topic>Glutenin</topic><topic>Heat shock proteins</topic><topic>Homology</topic><topic>inbred lines</topic><topic>Inbreeding</topic><topic>Life Sciences</topic><topic>Malate dehydrogenase</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Molecular biology</topic><topic>Molecular weight</topic><topic>Oxidative stress</topic><topic>Plant biology</topic><topic>Plant Genetics and Genomics</topic><topic>Plant Pathology</topic><topic>Plant Physiology</topic><topic>Plant Sciences</topic><topic>Protein folding</topic><topic>Proteins</topic><topic>proteomics</topic><topic>Quantitative trait loci</topic><topic>Regulatory proteins</topic><topic>Rubber</topic><topic>Rye</topic><topic>Scientific imaging</topic><topic>sequence homology</topic><topic>Spectroscopy</topic><topic>sprouting</topic><topic>structural genes</topic><topic>α-Amylase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Masojć, Piotr</creatorcontrib><creatorcontrib>Kosmala, Arkadiusz</creatorcontrib><collection>AGRIS</collection><collection>Springer Nature OA Free Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Agricultural Science Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular breeding</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Masojć, Piotr</au><au>Kosmala, Arkadiusz</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteomic analysis of preharvest sprouting in rye using two-dimensional electrophoresis and mass spectrometry</atitle><jtitle>Molecular breeding</jtitle><stitle>Mol Breeding</stitle><addtitle>Mol Breed</addtitle><date>2012-10-01</date><risdate>2012</risdate><volume>30</volume><issue>3</issue><spage>1355</spage><epage>1361</epage><pages>1355-1361</pages><issn>1380-3743</issn><eissn>1572-9788</eissn><abstract>Qualitative and quantitative differences were found between two-dimensional electrophoretic spectra of 546 proteins from two bulked samples of mature rye grain representing: (1) 20 recombinant inbred lines extremely resistant to preharvest sprouting and (2) 20 recombinant inbred lines extremely susceptible to preharvest sprouting. Mass spectrometry of resolved proteins showed that four spots specific for PHS susceptibility represented high molecular weight glutenin subunit, glutathione transferase, 16.9 kDa heat-shock protein, and monomeric alpha-amylase inhibitor. Two spots specific for PHS resistance contained cytosolic malate dehydrogenase and functionally unrecognized protein with sequence homology to rubber elongation factor protein. Majority of 14 proteins with at least two-fold higher accumulation level in preharvest sprouting susceptible lines relative to that found in sprouting resistant lines, showed sequence homology to proteins involved in defense mechanisms against biotic and abiotic stresses including oxidative stress, and those taking part in energy supply. Two spots were identified as regulatory proteins from the 14-3-3 family with one molecular form prevailing in sprouting susceptible and another form highly accumulated in sprouting resistant lines. Further study establishing map positions of the revealed structural genes in respect to quantitative trait loci for preharvest sprouting in rye should answer the question on their possible status as candidate genes.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><pmid>23024596</pmid><doi>10.1007/s11032-012-9721-z</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 14-3-3 protein alpha-amylase Amino acid sequence Biomedical and Life Sciences Biotechnology defense mechanisms Electrophoresis Elongation Gene mapping Genes Glutathione Glutathione transferase Glutenin Heat shock proteins Homology inbred lines Inbreeding Life Sciences Malate dehydrogenase Mass spectrometry Mass spectroscopy Molecular biology Molecular weight Oxidative stress Plant biology Plant Genetics and Genomics Plant Pathology Plant Physiology Plant Sciences Protein folding Proteins proteomics Quantitative trait loci Regulatory proteins Rubber Rye Scientific imaging sequence homology Spectroscopy sprouting structural genes α-Amylase |
| title | Proteomic analysis of preharvest sprouting in rye using two-dimensional electrophoresis and mass spectrometry |
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