de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Targeted Enhancement of Glutamate-to-gamma-Aminobutyrate Conversion in Arabidopsis Seeds Affects Carbon-Nitrogen Balance and Storage Reserves in a Development-Dependent Manner

Fait, A., Nunes Nesi, A., Angelovici, R., Lehmann, M., Pham, P. A., Song, L., et al. (2011). Targeted Enhancement of Glutamate-to-gamma-Aminobutyrate Conversion in Arabidopsis Seeds Affects Carbon-Nitrogen Balance and Storage Reserves in a Development-Dependent Manner. Plant Physiology, 157(3), 1026-1042. doi:10.1104/pp.111.179986.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-2216-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-839B-B
Genre: Journal Article

Files

show Files
hide Files
:
Fait-2011-Targeted Enhancement.pdf (Any fulltext), 2MB
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Fait, A.1, Author              
Nunes Nesi, A.2, Author
Angelovici, R.2, Author
Lehmann, M.1, Author              
Pham, P. A.1, Author              
Song, L.2, Author
Haslam, R. P.2, Author
Napier, J. A.2, Author
Galili, G.2, Author
Fernie, A. R.1, Author              
Affiliations:
1Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, escidoc:1753339              
2External Organizations, escidoc:persistent22              

Content

show
hide
Free keywords: calmodulin-binding domain developing soybean seeds fatty-acid synthesis amino-acids biochemical-characterization gas-chromatography metabolic networks fruit-development lysine synthesis brassica-napus
 Abstract: In seeds, glutamate decarboxylase (GAD) operates at the metabolic nexus between carbon and nitrogen metabolism by catalysing the unidirectional decarboxylation of Glu to form gamma-aminobutyric acid (GABA). To elucidate the regulatory role of GAD in seed development, we generated Arabidopsis thaliana transgenic plants expressing a truncated GAD from Petunia hybrida missing the C-terminal regulatory Ca2+-calmodulin (CaM) binding domain, under the transcriptional regulation of the seed maturation specific phaseolin promoter. Dry seeds of the transgenic plants accumulated considerable amounts of GABA, and during desiccation the content of several amino acids increased, though not Glu or Pro. Dry transgenic seeds had higher protein content than the wild-type seeds, but lower amounts of the intermediates of glycolysis, glycerol and malate. The total fatty acid (TFA) content of the transgenic seeds was 50% lower than in that of the wild-type, while acyl CoAs accumulated in the transgenic seeds. Labeling experiments revealed altered levels of respiration in the transgenic seeds, and fractionation studies indicated reduced incorporation of label in the sugar and lipid fractions extracted from transgenic seeds. Comparative transcript profiling of the dry seeds supported the metabolic data. Cellular processes upregulated at the transcript level included the tricarboxylic acid cycle, fatty acid elongation, the shikimate pathway and Trp metabolism, N-C remobilization and programmed cell death. Genes involved in the regulation of germination were similarly upregulated. Taken together these results indicate that the GAD-mediated conversion of Glu to GABA during seed development plays an important role in balancing carbon and nitrogen metabolism and in storage reserve accumulation.

Details

show
hide
Language(s): eng - English
 Dates: 2011-09-172011
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Plant Physiology
  Other : Plant Physiol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Bethesda, Md. : American Society of Plant Biologists
Pages: - Volume / Issue: 157 (3) Sequence Number: - Start / End Page: 1026 - 1042 Identifier: ISSN: 0032-0889
CoNE: http://pubman.mpdl.mpg.de/cone/journals/resource/991042744294438