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231223s2010 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erq179
|2 doi
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|a pubmed25n0663.xml
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|a (DE-627)NLM198918496
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|a (NLM)20558569
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Holding, David R
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Identification and characterization of the maize arogenate dehydrogenase gene family
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|c 2010
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| 336 |
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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 29.09.2010
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|a Date Revised 17.03.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a In plants, the amino acids tyrosine and phenylalanine are synthesized from arogenate by arogenate dehydrogenase and arogenate dehydratase, respectively, with the relative flux to each being tightly controlled. Here the characterization of a maize opaque endosperm mutant (mto140), which also shows retarded vegetative growth, is described The opaque phenotype co-segregates with a Mutator transposon insertion in an arogenate dehydrogenase gene (zmAroDH-1) and this led to the characterization of the four-member family of maize arogenate dehydrogenase genes (zmAroDH-1-zmAroDH-4) which share highly similar sequences. A Mutator insertion at an equivalent position in AroDH-3, the most closely related family member to AroDH-1, is also associated with opaque endosperm and stunted vegetative growth phenotypes. Overlapping but differential expression patterns as well as subtle mutant effects on the accumulation of tyrosine and phenylalanine in endosperm, embryo, and leaf tissues suggest that the functional redundancy of this gene family provides metabolic plasticity for the synthesis of these important amino acids. mto140/arodh-1 seeds shows a general reduction in zein storage protein accumulation and an elevated lysine phenotype typical of other opaque endosperm mutants, but it is distinct because it does not result from quantitative or qualitative defects in the accumulation of specific zeins but rather from a disruption in amino acid biosynthesis
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Amino Acids
|2 NLM
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|a Tyrosine
|2 NLM
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|a 42HK56048U
|2 NLM
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| 650 |
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|a Phenylalanine
|2 NLM
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| 650 |
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|a 47E5O17Y3R
|2 NLM
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| 650 |
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|a Zein
|2 NLM
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| 650 |
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|a 9010-66-6
|2 NLM
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| 650 |
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|a Prephenate Dehydrogenase
|2 NLM
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| 650 |
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|a EC 1.3.1.12
|2 NLM
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| 650 |
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|a cyclohexadienyl dehydrogenase
|2 NLM
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| 650 |
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|a EC 1.3.1.43
|2 NLM
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| 650 |
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|a Lysine
|2 NLM
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| 650 |
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|a K3Z4F929H6
|2 NLM
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| 700 |
1 |
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|a Meeley, Robert B
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Hazebroek, Jan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Selinger, David
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Gruis, Fred
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Jung, Rudolf
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Larkins, Brian A
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 61(2010), 13 vom: 01. Aug., Seite 3663-73
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
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|g volume:61
|g year:2010
|g number:13
|g day:01
|g month:08
|g pages:3663-73
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| 856 |
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|u http://dx.doi.org/10.1093/jxb/erq179
|3 Volltext
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|d 61
|j 2010
|e 13
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|c 08
|h 3663-73
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