Identification and characterization of lysine-rich proteins and starch biosynthesis genes in the opaque2 mutant by transcriptional and proteomic analysis

Persistent Link:
http://hdl.handle.net/10150/610085
Title:
Identification and characterization of lysine-rich proteins and starch biosynthesis genes in the opaque2 mutant by transcriptional and proteomic analysis
Author:
Jia, Mo; Wu, Hao; Clay, Kasi; Jung, Rudolf; Larkins, Brian; Gibbon, Bryan
Affiliation:
Department of Biology, Baylor University, One Bear place #97388, Waco, TX 76798, USA; Pioneer Hi-Bred International, Inc., Johnston, IA 50131, USA; Department of Plant Sciences, University of Arizona, Tucson, AZ 85721, USA
Issue Date:
2013
Publisher:
BioMed Central
Citation:
Jia et al. BMC Plant Biology 2013, 13:60 http://www.biomedcentral.com/1471-2229/13/60
Journal:
BMC Plant Biology
Rights:
© 2013 Jia et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0)
Collection Information:
This item is part of the UA Faculty Publications collection. For more information this item or other items in the UA Campus Repository, contact the University of Arizona Libraries at repository@u.library.arizona.edu.
Abstract:
BACKGROUND:The opaque2 mutant is valuable for producing maize varieties with enhanced nutritional value. However, the exact mechanisms by which it improves protein quality and creates a soft endosperm texture are unclear. Given the importance of improving nutritional quality in grain crops, a better understanding of the physiological basis for these traits is necessary.RESULTS:In this study, we combined transcript profiling and proteomic analysis to better understand which genes and proteins are altered by opaque2 in the W64A inbred line. These analyses showed that the accumulation of some lysine-rich proteins, such as sorbitol dehydrogenase and glyceraldehyde3-phosphate dehydrogenase, was increased in mature kernels and may contribute substantially to the lysine content of opaque2 endosperm. Some defense proteins such as beta-glucosidase aggregating factor were strongly down regulated and may be regulated directly by opaque2. The mutant also had altered expression of a number of starch biosynthesis genes and this was associated with a more highly crystalline starch.CONCLUSIONS:The results of these studies revealed specific target genes that can be investigated to further improve nutritional quality and agronomic performance of high lysine maize lines, particularly those based on the presence of the opaque2 mutation. Alteration of amylopectin branching patterns in opaque2 starch could contribute to generation of the soft, starchy endosperm.
EISSN:
1471-2229
DOI:
10.1186/1471-2229-13-60
Keywords:
Opaque endosperm; Opaque2; Quality protein maize; Starch biosynthesis; Protein quality
Version:
Final published version
Additional Links:
http://www.biomedcentral.com/1471-2229/13/60

Full metadata record

DC FieldValue Language
dc.contributor.authorJia, Moen
dc.contributor.authorWu, Haoen
dc.contributor.authorClay, Kasien
dc.contributor.authorJung, Rudolfen
dc.contributor.authorLarkins, Brianen
dc.contributor.authorGibbon, Bryanen
dc.date.accessioned2016-05-20T08:58:13Z-
dc.date.available2016-05-20T08:58:13Z-
dc.date.issued2013en
dc.identifier.citationJia et al. BMC Plant Biology 2013, 13:60 http://www.biomedcentral.com/1471-2229/13/60en
dc.identifier.doi10.1186/1471-2229-13-60en
dc.identifier.urihttp://hdl.handle.net/10150/610085-
dc.description.abstractBACKGROUND:The opaque2 mutant is valuable for producing maize varieties with enhanced nutritional value. However, the exact mechanisms by which it improves protein quality and creates a soft endosperm texture are unclear. Given the importance of improving nutritional quality in grain crops, a better understanding of the physiological basis for these traits is necessary.RESULTS:In this study, we combined transcript profiling and proteomic analysis to better understand which genes and proteins are altered by opaque2 in the W64A inbred line. These analyses showed that the accumulation of some lysine-rich proteins, such as sorbitol dehydrogenase and glyceraldehyde3-phosphate dehydrogenase, was increased in mature kernels and may contribute substantially to the lysine content of opaque2 endosperm. Some defense proteins such as beta-glucosidase aggregating factor were strongly down regulated and may be regulated directly by opaque2. The mutant also had altered expression of a number of starch biosynthesis genes and this was associated with a more highly crystalline starch.CONCLUSIONS:The results of these studies revealed specific target genes that can be investigated to further improve nutritional quality and agronomic performance of high lysine maize lines, particularly those based on the presence of the opaque2 mutation. Alteration of amylopectin branching patterns in opaque2 starch could contribute to generation of the soft, starchy endosperm.en
dc.language.isoenen
dc.publisherBioMed Centralen
dc.relation.urlhttp://www.biomedcentral.com/1471-2229/13/60en
dc.rights© 2013 Jia et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0)en
dc.subjectOpaque endospermen
dc.subjectOpaque2en
dc.subjectQuality protein maizeen
dc.subjectStarch biosynthesisen
dc.subjectProtein qualityen
dc.titleIdentification and characterization of lysine-rich proteins and starch biosynthesis genes in the opaque2 mutant by transcriptional and proteomic analysisen
dc.typeArticleen
dc.identifier.eissn1471-2229en
dc.contributor.departmentDepartment of Biology, Baylor University, One Bear place #97388, Waco, TX 76798, USAen
dc.contributor.departmentPioneer Hi-Bred International, Inc., Johnston, IA 50131, USAen
dc.contributor.departmentDepartment of Plant Sciences, University of Arizona, Tucson, AZ 85721, USAen
dc.identifier.journalBMC Plant Biologyen
dc.description.collectioninformationThis item is part of the UA Faculty Publications collection. For more information this item or other items in the UA Campus Repository, contact the University of Arizona Libraries at repository@u.library.arizona.edu.en
dc.eprint.versionFinal published versionen
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