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231224s2013 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2013.09.003
|2 doi
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|a pubmed24n0771.xml
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|a (DE-627)NLM231287844
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|a (NLM)24080395
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|a (PII)S0981-9428(13)00309-4
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Kang, Guozhang
|e verfasserin
|4 aut
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|a Increasing the starch content and grain weight of common wheat by overexpression of the cytosolic AGPase large subunit gene
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|c 2013
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 29.07.2014
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|a Date Revised 09.04.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2013 Elsevier Masson SAS. All rights reserved.
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|a ADP-glucose pyrophosphorylase (AGPase) catalyzes the first committed step of starch synthesis. AGPase is a heterotetramer composed of two large subunits and two small subunits, has cytosolic and plastidial isoforms, and is detected mainly in the cytosol of endosperm in cereal crops. To investigate the effects of AGPase cytosolic large subunit gene (LSU I) on starch biosynthesis in higher plant, in this study, a TaLSU I gene from wheat was overexpressed under the control of an endosperm-specific promoter in a wheat cultivar (Yumai 34). PCR, Southern blot, and real-time RT-PCR analyses indicated that the transgene was integrated into the genome of transgenic plants and was overexpressed in their progeny. The overexpression of the TaLSU I gene remarkably enhanced AGPase activity, endosperm starch weight, grain number per spike, and single grain weight. Therefore, we conclude that overexpression of the TaLSU I gene enhances the starch biosynthesis in endosperm of wheat grains, having potential applications in wheat breeding to develop a high-yield wheat cultivar with high starch weight and kernel weight
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a AGPase
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|a Cytosolic large subunit
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|a Overexpression
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|a Starch
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|a Wheat (Triticum aextivum L.)
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|a Plant Proteins
|2 NLM
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|a Protein Subunits
|2 NLM
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|a Starch
|2 NLM
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|a 9005-25-8
|2 NLM
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|a Glucose-1-Phosphate Adenylyltransferase
|2 NLM
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|a EC 2.7.7.27
|2 NLM
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| 700 |
1 |
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|a Liu, Guoqin
|e verfasserin
|4 aut
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| 700 |
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|a Peng, Xiaoqi
|e verfasserin
|4 aut
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| 700 |
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|a Wei, Liting
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wang, Chenyang
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhu, YunJi
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ma, Ying
|e verfasserin
|4 aut
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|a Jiang, Yumei
|e verfasserin
|4 aut
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| 700 |
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|a Guo, Tiancai
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 73(2013) vom: 01. Dez., Seite 93-8
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
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|g volume:73
|g year:2013
|g day:01
|g month:12
|g pages:93-8
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|u http://dx.doi.org/10.1016/j.plaphy.2013.09.003
|3 Volltext
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