Pullulanase and Starch Synthase III Are Associated with Formation of Vitreous Endosperm in Quality Protein Maize
The opaque-2 (o2) mutation of maize increases lysine content, but the low seed density and soft texture of this type of mutant are undesirable. Lines with modifiers of the soft kernel phenotype (mo2) called "Quality Protein Maize" (QPM) have high lysine and kernel phenotypes similar to nor...
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description | The opaque-2 (o2) mutation of maize increases lysine content, but the low seed density and soft texture of this type of mutant are undesirable. Lines with modifiers of the soft kernel phenotype (mo2) called "Quality Protein Maize" (QPM) have high lysine and kernel phenotypes similar to normal maize. Prior research indicated that the formation of vitreous endosperm in QPM might involve changes in starch granule structure. In this study, we focused on analysis of two starch biosynthetic enzymes that may influence kernel vitreousness. Analysis of recombinant inbred lines derived from a cross of W64Ao2 and K0326Y revealed that pullulanase activity had significant positive correlation with kernel vitreousness. We also found that decreased Starch Synthase III abundance may decrease the pullulanase activity and average glucan chain length given the same Zpu1 genotype. Therefore, Starch Synthase III could indirectly influence the kernel vitreousness by affecting pullulanase activity and coordinating with pullulanase to alter the glucan chain length distribution of amylopectin, resulting in different starch structural properties. The glucan chain length distribution had strong positive correlation with the polydispersity index of glucan chains, which was positively associated with the kernel vitreousness based on nonlinear regression analysis. Therefore, we propose that pullulanase and Starch Synthase III are two important factors responsible for the formation of the vitreous phenotype of QPM endosperms. |
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Lines with modifiers of the soft kernel phenotype (mo2) called "Quality Protein Maize" (QPM) have high lysine and kernel phenotypes similar to normal maize. Prior research indicated that the formation of vitreous endosperm in QPM might involve changes in starch granule structure. In this study, we focused on analysis of two starch biosynthetic enzymes that may influence kernel vitreousness. Analysis of recombinant inbred lines derived from a cross of W64Ao2 and K0326Y revealed that pullulanase activity had significant positive correlation with kernel vitreousness. We also found that decreased Starch Synthase III abundance may decrease the pullulanase activity and average glucan chain length given the same Zpu1 genotype. Therefore, Starch Synthase III could indirectly influence the kernel vitreousness by affecting pullulanase activity and coordinating with pullulanase to alter the glucan chain length distribution of amylopectin, resulting in different starch structural properties. The glucan chain length distribution had strong positive correlation with the polydispersity index of glucan chains, which was positively associated with the kernel vitreousness based on nonlinear regression analysis. Therefore, we propose that pullulanase and Starch Synthase III are two important factors responsible for the formation of the vitreous phenotype of QPM endosperms.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0130856</identifier><identifier>PMID: 26115014</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino acids ; Amylopectin ; Analysis ; Biology ; Biosynthesis ; Chains ; Corn ; Correlation ; Endosperm ; Endosperm - metabolism ; Enzymes ; Gene expression ; Genotypes ; Glucan ; Glycoside Hydrolases - metabolism ; Inbreeding ; Lysine ; Microscopy ; Molecular conformation ; Mutation ; Nonlinear analysis ; Phenotypes ; Plant Proteins - metabolism ; Polydispersity ; Polymers ; Proteins ; Pullulanase ; Regression analysis ; Starch ; Starch synthase ; Starch Synthase - metabolism ; Starch synthase III ; Zea mays - enzymology</subject><ispartof>PloS one, 2015-06, Vol.10 (6), p.e0130856-e0130856</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Wu et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015 Wu et al 2015 Wu et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-8a256a5dae61b787910f9c5a0ff58a213cbc105deb5aa7c30aa3ed8011c7aa033</citedby><cites>FETCH-LOGICAL-c692t-8a256a5dae61b787910f9c5a0ff58a213cbc105deb5aa7c30aa3ed8011c7aa033</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4482715/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4482715/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26115014$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Ma, Wujun</contributor><creatorcontrib>Wu, Hao</creatorcontrib><creatorcontrib>Clay, Kasi</creatorcontrib><creatorcontrib>Thompson, Stephanie S</creatorcontrib><creatorcontrib>Hennen-Bierwagen, Tracie A</creatorcontrib><creatorcontrib>Andrews, Bethany J</creatorcontrib><creatorcontrib>Zechmann, Bernd</creatorcontrib><creatorcontrib>Gibbon, Bryan C</creatorcontrib><title>Pullulanase and Starch Synthase III Are Associated with Formation of Vitreous Endosperm in Quality Protein Maize</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The opaque-2 (o2) mutation of maize increases lysine content, but the low seed density and soft texture of this type of mutant are undesirable. Lines with modifiers of the soft kernel phenotype (mo2) called "Quality Protein Maize" (QPM) have high lysine and kernel phenotypes similar to normal maize. Prior research indicated that the formation of vitreous endosperm in QPM might involve changes in starch granule structure. In this study, we focused on analysis of two starch biosynthetic enzymes that may influence kernel vitreousness. Analysis of recombinant inbred lines derived from a cross of W64Ao2 and K0326Y revealed that pullulanase activity had significant positive correlation with kernel vitreousness. We also found that decreased Starch Synthase III abundance may decrease the pullulanase activity and average glucan chain length given the same Zpu1 genotype. Therefore, Starch Synthase III could indirectly influence the kernel vitreousness by affecting pullulanase activity and coordinating with pullulanase to alter the glucan chain length distribution of amylopectin, resulting in different starch structural properties. The glucan chain length distribution had strong positive correlation with the polydispersity index of glucan chains, which was positively associated with the kernel vitreousness based on nonlinear regression analysis. Therefore, we propose that pullulanase and Starch Synthase III are two important factors responsible for the formation of the vitreous phenotype of QPM endosperms.</description><subject>Amino acids</subject><subject>Amylopectin</subject><subject>Analysis</subject><subject>Biology</subject><subject>Biosynthesis</subject><subject>Chains</subject><subject>Corn</subject><subject>Correlation</subject><subject>Endosperm</subject><subject>Endosperm - metabolism</subject><subject>Enzymes</subject><subject>Gene expression</subject><subject>Genotypes</subject><subject>Glucan</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Inbreeding</subject><subject>Lysine</subject><subject>Microscopy</subject><subject>Molecular conformation</subject><subject>Mutation</subject><subject>Nonlinear analysis</subject><subject>Phenotypes</subject><subject>Plant Proteins - metabolism</subject><subject>Polydispersity</subject><subject>Polymers</subject><subject>Proteins</subject><subject>Pullulanase</subject><subject>Regression analysis</subject><subject>Starch</subject><subject>Starch synthase</subject><subject>Starch Synthase - metabolism</subject><subject>Starch synthase III</subject><subject>Zea mays - enzymology</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk99v0zAQxyMEYmPwHyCwhITgocWOfyR5QaqmDSINbVDYq3VxnNZTGhfbAcpfj0OzqUF7QH6wffe5r31nX5I8J3hOaEbe3djeddDOt7bTc0wozrl4kByTgqYzkWL68GB9lDzx_gZjTnMhHidHqSCEY8KOk-1V37Z9Cx14jaCr0TKAU2u03HVhPdjKskQLp9HCe6sMBF2jnyas0bl1GwjGdsg26NoEp23v0VlXW7_VboNMhz730JqwQ1fOBh33n8D81k-TRw20Xj8b55Pk2_nZ19OPs4vLD-Xp4mKmRJGGWQ4pF8Br0IJUWZ4VBDeF4oCbhkcfoapSBPNaVxwgUxQDUF3nmBCVAWBKT5KXe91ta70ci-UlEQVhOM9THolyT9QWbuTWmQ24nbRg5F-DdSsJLhjVaslEU6SiqYCmnOWa5IwVmlW8opVSjVJR6_14Wl9tdK10Fxy0E9GppzNrubI_JGN5mpHhMm9GAWe_99oHuTFe6Ta-zFDY4d5pWrAMs4i--ge9P7uRWkFMwHSNjeeqQVQuGCk4FoSJSM3voeKo9cao-LMaE-2TgLeTgMgE_SusoPdelssv_89eXk_Z1wfsWkMb1t62_fDD_BRke1A5673TzV2RCZZDY9xWQw6NIcfGiGEvDh_oLui2E-gf6kEJGA</recordid><startdate>20150626</startdate><enddate>20150626</enddate><creator>Wu, Hao</creator><creator>Clay, Kasi</creator><creator>Thompson, Stephanie S</creator><creator>Hennen-Bierwagen, Tracie A</creator><creator>Andrews, Bethany J</creator><creator>Zechmann, Bernd</creator><creator>Gibbon, Bryan C</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20150626</creationdate><title>Pullulanase and Starch Synthase III Are Associated with Formation of Vitreous Endosperm in Quality Protein Maize</title><author>Wu, Hao ; Clay, Kasi ; Thompson, Stephanie S ; Hennen-Bierwagen, Tracie A ; Andrews, Bethany J ; Zechmann, Bernd ; Gibbon, Bryan C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-8a256a5dae61b787910f9c5a0ff58a213cbc105deb5aa7c30aa3ed8011c7aa033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Amino acids</topic><topic>Amylopectin</topic><topic>Analysis</topic><topic>Biology</topic><topic>Biosynthesis</topic><topic>Chains</topic><topic>Corn</topic><topic>Correlation</topic><topic>Endosperm</topic><topic>Endosperm - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, Hao</au><au>Clay, Kasi</au><au>Thompson, Stephanie S</au><au>Hennen-Bierwagen, Tracie A</au><au>Andrews, Bethany J</au><au>Zechmann, Bernd</au><au>Gibbon, Bryan C</au><au>Ma, Wujun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pullulanase and Starch Synthase III Are Associated with Formation of Vitreous Endosperm in Quality Protein Maize</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-06-26</date><risdate>2015</risdate><volume>10</volume><issue>6</issue><spage>e0130856</spage><epage>e0130856</epage><pages>e0130856-e0130856</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The opaque-2 (o2) mutation of maize increases lysine content, but the low seed density and soft texture of this type of mutant are undesirable. Lines with modifiers of the soft kernel phenotype (mo2) called "Quality Protein Maize" (QPM) have high lysine and kernel phenotypes similar to normal maize. Prior research indicated that the formation of vitreous endosperm in QPM might involve changes in starch granule structure. In this study, we focused on analysis of two starch biosynthetic enzymes that may influence kernel vitreousness. Analysis of recombinant inbred lines derived from a cross of W64Ao2 and K0326Y revealed that pullulanase activity had significant positive correlation with kernel vitreousness. We also found that decreased Starch Synthase III abundance may decrease the pullulanase activity and average glucan chain length given the same Zpu1 genotype. Therefore, Starch Synthase III could indirectly influence the kernel vitreousness by affecting pullulanase activity and coordinating with pullulanase to alter the glucan chain length distribution of amylopectin, resulting in different starch structural properties. The glucan chain length distribution had strong positive correlation with the polydispersity index of glucan chains, which was positively associated with the kernel vitreousness based on nonlinear regression analysis. Therefore, we propose that pullulanase and Starch Synthase III are two important factors responsible for the formation of the vitreous phenotype of QPM endosperms.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26115014</pmid><doi>10.1371/journal.pone.0130856</doi><oa>free_for_read</oa></addata></record> |
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subjects | Amino acids Amylopectin Analysis Biology Biosynthesis Chains Corn Correlation Endosperm Endosperm - metabolism Enzymes Gene expression Genotypes Glucan Glycoside Hydrolases - metabolism Inbreeding Lysine Microscopy Molecular conformation Mutation Nonlinear analysis Phenotypes Plant Proteins - metabolism Polydispersity Polymers Proteins Pullulanase Regression analysis Starch Starch synthase Starch Synthase - metabolism Starch synthase III Zea mays - enzymology |
title | Pullulanase and Starch Synthase III Are Associated with Formation of Vitreous Endosperm in Quality Protein Maize |
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