Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Database
Language
Publication year range
1.
Plant Biotechnol J ; 20(6): 1140-1153, 2022 06.
Article in English | MEDLINE | ID: mdl-35244326

ABSTRACT

Maize is one of the world's most widely cultivated crops. As future demands for maize will continue to rise, fields will face ever more frequent and extreme weather patterns that directly affect crop productivity. Development of environmentally resilient crops with improved standability in the field, like wheat and rice, was enabled by shifting the architecture of plants to a short stature ideotype. However, such architectural change has not been implemented in maize due to the unique interactions between gibberellin (GA) and floral morphology which limited the use of the same type of mutations as in rice and wheat. Here, we report the development of a short stature maize ideotype in commercial hybrid germplasm, which was generated by targeted suppression of the biosynthetic pathway for GA. To accomplish this, we utilized a dominant, miRNA-based construct expressed in a hemizygous state to selectively reduce expression of the ZmGA20ox3 and ZmGA20ox5 genes that control GA biosynthesis primarily in vegetative tissues. Suppression of both genes resulted in the reduction of GA levels leading to inhibition of cell elongation in internodal tissues, which reduced plant height. Expression of the miRNA did not alter GA levels in reproductive tissues, and thus, the reproductive potential of the plants remained unchanged. As a result, we developed a dominant, short-stature maize ideotype that is conducive for the commercial production of hybrid maize. We expect that the new maize ideotype would enable more efficient and more sustainable maize farming for a growing world population.


Subject(s)
MicroRNAs , Oryza , Crops, Agricultural/genetics , Gibberellins/metabolism , MicroRNAs/genetics , MicroRNAs/metabolism , Oryza/genetics , Plant Proteins , Triticum/genetics , Zea mays/metabolism
2.
Metab Eng ; 13(1): 96-107, 2011 Jan.
Article in English | MEDLINE | ID: mdl-20969971

ABSTRACT

¹4C labeling experiments performed with kernel cultures showed that developing maize endosperm is more efficient than other non-photosynthetic tissues such as sunflower and maize embryos at converting maternally supplied substrates into biomass. To characterize the metabolic fluxes in endosperm, maize kernels were labeled to isotopic steady state using ¹³C-labeled glucose. The resultant labeling in free metabolites and biomass was analyzed by NMR and GC-MS. After taking into account the labeling of substrates supplied by the metabolically active cob, the fluxes through central metabolism were quantified by computer-aided modeling. The flux map indicates that 51-69% of the ATP produced is used for biomass synthesis and up to 47% is expended in substrate cycling. These findings point to potential engineering targets for improving yield and increasing oil contents by, respectively, reducing substrate cycling and increasing the commitment of plastidic carbon into fatty acid synthesis at the level of pyruvate kinase.


Subject(s)
Carbon Isotopes/pharmacokinetics , Endosperm/metabolism , Gene Targeting/methods , Models, Biological , Plant Proteins/metabolism , Signal Transduction/physiology , Zea mays/metabolism , Computer Simulation , Endosperm/genetics , Endosperm/growth & development , Metabolic Clearance Rate , Plant Proteins/genetics , Plants, Genetically Modified/genetics , Plants, Genetically Modified/metabolism , Protein Engineering/methods , Zea mays/genetics , Zea mays/growth & development
3.
Mol Cell ; 9(3): 685-94, 2002 Mar.
Article in English | MEDLINE | ID: mdl-11931774

ABSTRACT

Synthesis and detection of acyl-homoserine lactones (AHLs) enables many gram-negative bacteria to engage in quorum sensing, an intercellular signaling mechanism that activates differentiation to virulent and biofilm lifestyles. The AHL synthases catalyze acylation of S-adenosyl-L-methionine by acyl-acyl carrier protein and lactonization of the methionine moiety to give AHLs. The crystal structure of the AHL synthase, EsaI, determined at 1.8 A resolution, reveals a remarkable structural similarity to the N-acetyltransferases and defines a common phosphopantetheine binding fold as the catalytic core. Critical residues responsible for catalysis and acyl chain specificity have been identified from a modeled substrate complex and verified through functional analysis in vivo. A mechanism for the N-acylation of S-adenosyl-L-methionine by 3-oxo-hexanoyl-acyl carrier protein is proposed.


Subject(s)
4-Butyrolactone/biosynthesis , Bacterial Proteins/chemistry , Gram-Negative Bacteria/enzymology , Signal Transduction , 4-Butyrolactone/analogs & derivatives , Amino Acid Sequence , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Binding Sites , Gram-Negative Bacteria/genetics , Models, Molecular , Molecular Sequence Data , Molecular Structure , Mutagenesis, Site-Directed , Protein Structure, Tertiary , Sequence Alignment , Substrate Specificity
SELECTION OF CITATIONS
SEARCH DETAIL
...