Entity

Time filter

Source Type


Lu S.,King Abdullah University of Science and Technology | Zhao H.,King Abdullah University of Science and Technology | Parsons E.P.,Purdue University | Xu C.,Brookhaven National Laboratory | And 8 more authors.
Plant Physiology | Year: 2011

A novel mutant of Arabidopsis (Arabidopsis thaliana), having highly glossy inflorescence stems, postgenital fusion in floral organs, and reduced fertility, was isolated from an ethyl methanesulfonate-mutagenized population and designated glossyhead1 (gsd1). The gsd1 locus was mapped to chromosome 1, and the causal gene was identified as a new allele of Acetyl-Coenzyme A Carboxylase1 (ACC1), a gene encoding the main enzyme in cytosolic malonyl-coenzyme A synthesis. This, to our knowledge, is the first mutant allele of ACC1 that does not cause lethality at the seed or early germination stage, allowing for the first time a detailed analysis of ACC1 function in mature tissues. Broad lipid profiling of mature gsd1 organs revealed a primary role for ACC1 in the biosynthesis of the very-long-chain fatty acids (C 20:0 or longer) associated with cuticular waxes and triacylglycerols. Unexpectedly, transcriptome analysis revealed that gsd1 has limited impact on any lipid metabolic networks but instead has a large effect on environmental stress-responsive pathways, especially senescence and ethylene synthesis determinants, indicating a possible role for the cytosolic malonyl-coenzyme A-derived lipids in stress response signaling. © 2011 American Society of Plant Biologists. All Rights Reserved. Source


Groenendyk D.G.,University of Arizona | Ferre T.P.A.,University of Arizona | Thorp K.R.,United States Arid Land Agricultural Research Center | Rice A.K.,Colorado School of Mines
PLoS ONE | Year: 2015

Soils lie at the interface between the atmosphere and the subsurface and are a key component that control ecosystem services, food production, and many other processes at the Earth's surface. There is a long-established convention for identifying and mapping soils by texture. These readily available, georeferenced soil maps and databases are used widely in environmental sciences. Here, we show that these traditional soil classifications can be inappropriate, contributing to bias and uncertainty in applications from slope stability to water resource management. We suggest a new approach to soil classification, with a detailed example from the science of hydrology. Hydrologic simulations based on common meteorological conditions were performed using HYDRUS-1D, spanning textures identified by the United States Department of Agriculture soil texture triangle. We consider these common conditions to be: drainage from saturation, infiltration onto a drained soil, and combined infiltration and drainage events. Using a k-means clustering algorithm, we created soil classifications based on the modeled hydrologic responses of these soils. The hydrologic-process-based classifications were compared to those based on soil texture and a single hydraulic property, Ks. Differences in classifications based on hydrologic response versus soil texture demonstrate that traditional soil texture classification is a poor predictor of hydrologic response. We then developed a QGIS plugin to construct soil maps combining a classification with georeferenced soil data from the Natural Resource Conservation Service. The spatial patterns of hydrologic response were more immediately informative, much simpler, and less ambiguous, for use in applications ranging from trafficability to irrigation management to flood control. The ease with which hydrologic-process-based classifications can be made, along with the improved quantitative predictions of soil responses and visualization of landscape function, suggest that hydrologic-process-based classifications should be incorporated into environmental process models and can be used to define application-specific maps of hydrologic function. © 2015, Public Library of Science. All rights reserved. This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. Source


Horn P.J.,University of North Texas | James C.N.,University of North Texas | Gidda S.K.,University of Guelph | Kilaru A.,East Tennessee State University | And 5 more authors.
Plant Physiology | Year: 2013

Lipid droplets in plants (also known as oil bodies, lipid bodies, or oleosomes) are well characterized in seeds, and oleosins, the major proteins associated with their surface, were shown to be important for stabilizing lipid droplets during seed desiccation and rehydration. However, lipid droplets occur in essentially all plant cell types, many of which may not require oleosinmediated stabilization. The proteins associated with the surface of nonseed lipid droplets, which are likely to influence the formation, stability, and turnover of this compartment, remain to be elucidated. Here, we have combined lipidomic, proteomic, and transcriptomic studies of avocado (Persea americana) mesocarp to identify two new lipid droplet-associated proteins, which we named LDAP1 and LDAP2. These proteins are highly similar to each other and also to the small rubber particle proteins that accumulate in rubber-producing plants. An Arabidopsis (Arabidopsis thaliana) homolog to LDAP1 and LDAP2, At3g05500, was localized to the surface of lipid droplets after transient expression in tobacco (Nicotiana tabacum) cells that were induced to accumulate triacylglycerols. We propose that small rubber particle protein-like proteins are involved in the general process of binding and perhaps the stabilization of lipid-rich particles in the cytosol of plant cells and that the avocado and Arabidopsis protein members reveal a new aspect of the cellular machinery that is involved in the packaging of triacylglycerols in plant tissues. © 2013 American Society of Plant Biologists. All Rights Reserved. Source


Lu S.,King Abdullah University of Science and Technology | Zhao H.,King Abdullah University of Science and Technology | Des Marais D.L.,University of Texas at Austin | Parsons E.P.,Purdue University | And 9 more authors.
Plant Physiology | Year: 2012

Mutation of the ECERIFERUM9 (CER9) gene in Arabidopsis (Arabidopsis thaliana) causes elevated amounts of 18-carbon-length cutin monomers and a dramatic shift in the cuticular wax profile (especially on leaves) toward the very-long-chain free fatty acids tetracosanoic acid (C24) and hexacosanoic acid (C26). Relative to the wild type, cer9 mutants exhibit elevated cuticle membrane thickness over epidermal cells and cuticular ledges with increased occlusion of the stomatal pore. The cuticular phenotypes of cer9 are associated with delayed onset of wilting in plants experiencing water deficit, lower transpiration rates, and improved water use efficiency measured as carbon isotope discrimination. The CER9 protein thus encodes a novel determinant of plant drought tolerance-associated traits, one whose deficiency elevates cutin synthesis, redistributes wax composition, and suppresses transpiration. Map-based cloning identified CER9, and sequence analysis predicted that it encodes an E3 ubiquitin ligase homologous to yeast Doa10 (previously shown to target endoplasmic reticulum proteins for proteasomal degradation). To further elucidate CER9 function, the impact of CER9 deficiency on interactions with other genes was examined using double mutant and transcriptome analyses. For both wax and cutin, cer9 showed mostly additive effects with cer6, long-chain acyl-CoA synthetase1 (lacs1), and lacs2 and revealed its role in early steps of both wax and cutin synthetic pathways. Transcriptome analysis revealed that the cer9 mutation affected diverse cellular processes, with primary impact on genes associated with diverse stress responses. The discovery of CER9 lays new groundwork for developing novel cuticle-based strategies for improving the drought tolerance and water use efficiency of crop plants. © 2012 American Society of Plant Biologists. All Rights Reserved. Source


Lager I.,Swedish University of Agricultural Sciences | Yilmaz J.L.,Scandinavian Biotechnology Research AB | Zhou X.-R.,CSIRO | Jasieniecka K.,Medical University of Gdansk | And 12 more authors.
Journal of Biological Chemistry | Year: 2013

Background: Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine. Results: Plant LPCATs were expressed in yeast and biochemically characterized. Conclusion: LPCATs can edit acyl composition of phosphatidylcholine through their combined forward and reverse reactions. Significance: Plant LPCATs play a role in editing both sn-positions of PC and remove ricinoleic acid with high selectivity from this lipid. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. Source

Discover hidden collaborations