Research groups from Iowa State University and the Salk Institutefor Biological Studies have uncovered the function of three plantproteins, a discovery that could help plant scientists boost seedoil production in crops, thereby benefitting the production offood, biorenewable chemicals and biofuels. The analysis of gene activity (by the Iowa group) and determinationof protein structures (by the Salk group) independently identifiedin the model plant thale cress (Arabidopsis thaliana) three relatedproteins that appear to be involved in fatty-acid metabolism. TheIowa and Salk researchers then joined forces to test thishypothesis, demonstrating a role of these proteins in regulatingthe amounts and types of fatty acids accumulated in plants. The researchers also showed that the action of the proteins is verysensitive to temperature and that this feature may play animportant role in how plants mitigate temperature stress usingfatty acids. The discovery is published online at nature.com, the website of thejournal Nature. |
Corresponding authors are Eve Syrkin Wurtele, aprofessor of genetics, development and cell biology at Iowa State;and Joseph Noel, a professor and director of the Jack H. SkirballCenter for Chemical Biology and Proteomics at the Salk Institute inLa Jolla, Calif., and an investigator with the Howard HughesMedical Institute. "This work has major implications for modulating the fatty-acidprofiles in plants, which is terribly important, not only tosustainable food production and nutrition but now also tobiorenewable chemicals and fuels," Noel said. "Because very high-energy molecules such as fatty acids are createdin the plant using the energy of the sun, these types of moleculesmay ultimately provide the most cost-effective and efficientsources for biorenewable products," Wurtele added.
Although the researchers now understand that the three proteins -dubbed fatty-acid-binding proteins one, two and three, or FAP1,FAP2 and FAP3 - are involved in fatty-acid accumulation in planttissues such as leaves and seeds, Wurtele said researchers stilldon't understand the physical mechanism these proteins employ atthe molecular level. That knowledge will ultimately allow the twocollaborating research groups to predictably engineer betterfunctions in plants. To identify the proteins' function in plants, Wurtele's researchgroup used its expertise in molecular biology and bioinformatics(the application of computer technologies to biological studies). One tool the Iowa State researchers used was MetaOmGraph, softwarethey developed to analyze large sets of public data about thepatterns of gene activity under different developmental,environmental and genetic changes. The software revealed that theexpression patterns of the FAP genes resemble those of genesencoding enzymes of fatty-acid synthesis.
The analyses also showed that the accumulation of two of theproteins is highest in the regions of the plant where the greatestamount of oil is produced. These clues led the researchers topredict that the three FAP proteins are important for fatty-acidaccumulation. The Iowa State researchers then tested this theory experimentallyby comparing the fatty acids of mutant plants lacking the FAPproteins to those of normal plants. Despite the healthy appearanceof the mutant plants, the overall fatty-acid content is greaterthan in the normal plants, and the types of fatty acids differ. Noel and researchers at the Salk Institute used a variety oftechniques - including X-ray crystallography and biochemistry - tocharacterize the structures of the FAP1, FAP2 and FAP3 proteins,and to determine that the proteins bind fatty acids.
"The proteins appear to be crucial missing links in the metabolismof fatty acids in Arabidopsis, and likely serve a similar functionin other plant species since we find the same genes spreadthroughout the plant kingdom," said Ryan Philippe, a post-doctoralresearcher in Noel's lab. The project was supported in part by the National ScienceFoundation including the Engineering Research Center forBiorenewable Chemicals based at Iowa State, the National CancerInstitute, the Howard Hughes Medical Institute and Ngaki'sFulbright award. Additional support came from Iowa State's PlantSciences Institute. Discovery of the connection between the FAP proteins and plantfatty acids could be very useful to plant scientists.
"If the researchers can understand precisely what role the proteinsplay in seed oil production," said Ngaki, "they might be able tomodify the proteins' activity in new plant strains that producemore oil or higher quality oil than current crops." Further, if the three proteins help plants regulate stress, plantscientists might be able to exploit that trait to develop plantsthat are more resistant to stress, Wurtele said. And that couldallow farmers to grow crops for biorenewable fuels and chemicals onmarginal land that's not suited for food crops. All of this, she said, could point to new directions in biologicalstudies. "We are entering the age of predictive biology," Wurtele said."That means harnessing computational approaches to deduce genefunction, model biological processes and predict the consequencesof altering a single gene to the complex biological network of anorganism." Evolution of the chalcone isomerase fold from fattyacid-binding to stereospecific catalysis First authors of the paper are Micheline Ngaki, a Fulbright Scholarfrom the Congo and a graduate student in genetics, development andcell biology at Iowa State; Gordon Louie, a research scientist atthe Salk Institute; and Philippe. Other collaborators include LingLi, an Iowa State adjunct assistant professor and associatescientist in genetics, development and cell biology; GerardManning, director of Salk's Razavi Newman Center forBioinformatics; and Marianne Bowman, Florence Pojer and EliseLarsen, Howard Hughes Medical Institute researchers in the Salk'sSkirball Center.
Paper available here .
The e-commerce company in China offers quality products such as Silica Refractory , Corundum Refractory, and more. For more , please visit Ceramic Fiber Refractory today!
Related Articles -
Silica Refractory, Corundum Refractory,