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1.
Plant Biotechnol J ; 12(7): 941-50, 2014 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-24851925

RESUMEN

Grain yield from maize hybrids continues to improve through advances in breeding and biotechnology. Despite genetic improvements to hybrid maize, grain yield from distinct maize hybrids is expected to vary across growing locations due to numerous environmental factors. In this study, we examine across-location variation in grain yield among maize hybrids in three case studies. The three case studies examine hybrid improvement through breeding, introduction of an insect protection trait or introduction of a transcription factor trait associated with increased yield. In all cases, grain yield from each hybrid population had a Gaussian distribution. Across-location distributions of grain yield from each hybrid partially overlapped. The hybrid with a higher mean grain yield typically outperformed its comparator at most, but not all, of the growing locations (a 'win rate'). These results suggest that a broad set of environmental factors similarly impacts grain yields from both conventional- and biotechnology-derived maize hybrids and that grain yields among two or more hybrids should be compared with consideration given to both mean yield performance and the frequency of locations at which each hybrid 'wins' against its comparators. From an economic standpoint, growers recognize the value of genetically improved maize hybrids that outperform comparators in the majority of locations. Grower adoption of improved maize hybrids drives increases in average U.S. maize grain yields and contributes significant value to the economy.


Asunto(s)
Plantas Modificadas Genéticamente/crecimiento & desarrollo , Zea mays/genética , Agricultura/economía , Agricultura/tendencias , Cruzamiento , Hibridación Genética , Zea mays/crecimiento & desarrollo
2.
PLoS One ; 9(4): e94238, 2014.
Artículo en Inglés | MEDLINE | ID: mdl-24736658

RESUMEN

ATHB17 (AT2G01430) is an Arabidopsis gene encoding a member of the α-subclass of the homeodomain leucine zipper class II (HD-Zip II) family of transcription factors. The ATHB17 monomer contains four domains common to all class II HD-Zip proteins: a putative repression domain adjacent to a homeodomain, leucine zipper, and carboxy terminal domain. However, it also possesses a unique N-terminus not present in other members of the family. In this study we demonstrate that the unique 73 amino acid N-terminus is involved in regulation of cellular localization of ATHB17. The ATHB17 protein is shown to function as a transcriptional repressor and an EAR-like motif is identified within the putative repression domain of ATHB17. Transformation of maize with an ATHB17 expression construct leads to the expression of ATHB17Δ113, a truncated protein lacking the first 113 amino acids which encodes a significant portion of the repression domain. Because ATHB17Δ113 lacks the repression domain, the protein cannot directly affect the transcription of its target genes. ATHB17Δ113 can homodimerize, form heterodimers with maize endogenous HD-Zip II proteins, and bind to target DNA sequences; thus, ATHB17Δ113 may interfere with HD-Zip II mediated transcriptional activity via a dominant negative mechanism. We provide evidence that maize HD-Zip II proteins function as transcriptional repressors and that ATHB17Δ113 relieves this HD-Zip II mediated transcriptional repression activity. Expression of ATHB17Δ113 in maize leads to increased ear size at silking and, therefore, may enhance sink potential. We hypothesize that this phenotype could be a result of modulation of endogenous HD-Zip II pathways in maize.


Asunto(s)
Proteínas de Arabidopsis/genética , Proteínas de Arabidopsis/metabolismo , Eliminación de Secuencia/genética , Factores de Transcripción/genética , Factores de Transcripción/metabolismo , Zea mays/crecimiento & desarrollo , Zea mays/genética , Transporte Activo de Núcleo Celular , Secuencias de Aminoácidos , Secuencia de Aminoácidos , Proteínas de Arabidopsis/química , Peso Corporal/genética , Núcleo Celular/metabolismo , Secuencia de Consenso , Expresión Génica , Datos de Secuencia Molecular , Multimerización de Proteína , Estructura Cuaternaria de Proteína , Protoplastos/metabolismo , Reproducción , Factores de Transcripción/química , Transcripción Genética , Zea mays/citología , Zea mays/fisiología
3.
Bioorg Med Chem Lett ; 12(13): 1743-6, 2002 Jul 08.
Artículo en Inglés | MEDLINE | ID: mdl-12067551

RESUMEN

Imidazole glycerol phosphate dehydratase (IGPD) has become an attractive target for herbicide discovery since it is present in plants and not in mammals. Currently no knowledge is available on the 3-D structure of the IGPD active site. Therefore, we used a pharmacophore model based on known inhibitors and 3-D database searches to identify new active compounds. In vitro testing of compounds from the database searches led to the identification of a class of pyrrole aldehydes as novel inhibitors of IGPD.


Asunto(s)
Inhibidores Enzimáticos/química , Hidroliasas/antagonistas & inhibidores , Hidroliasas/química , Pirroles/química , Triazoles/química , Aldehídos/análisis , Aldehídos/química , Sitios de Unión , Bases de Datos Factuales , Herbicidas/química , Concentración 50 Inhibidora , Modelos Químicos , Conformación Molecular , Pirroles/análisis
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