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University of Wyoming

UW Technologies Available for Licensing


Technology Disclosure: 00-005 Controlling Plant Translation


Background

Translational control is a reversible, rapid and highly discriminating mechanism of cellular metabolic regulation. In yeasts and mammals, translational level control has been implicated in many diverse physiological events. One of the best characterized translational control mechanisms is the phosphorylation/dephosphorylation of the eIF2α protein. In most classes of eukaryotes this pathway has been demonstrated to be of significant importance in the regulation of critical processes like viral infection, biotic and abiotic stress response, cell division, and general cellular homeostasis. Unfortunately, very little is known in the literature regarding eIF2α translational regulation of plant growth and development.


Summary

Researchers in the University of Wyoming’s Department of Molecular Biology have elucidated the eIF2α pathway in plants and have identified and characterized its major components in two species (Arabidopsis and tobacco). Their work has shown compelling results with over-expression, under-expression, and inducible expression of this gene and its related gene product (in its phosphorylated and dephosphorylated states). For example, they have observed that the effect of constitutive overexpression of ‘phosphorylatable’ eIF2α (called 51S) has been to dramatically enhance growth. Such plants have been shown to grow 35-50% faster and have a biomass 15-20% greater than wildtype plants. They also have faster seed set and maturity rates. Conversely, constitutive over-expression of ‘non-phosphorylatable’ eIF2α (a mutant – called 51A) results in plants that mature 30-35% slower than controls. Yields are similarly decreased. Plant morphology is identical to controls for both 51S and 51A plants and all phenotypes are heritable. Work is on-going to target the improvement of specific agronomic traits using more precise molecular control (with inducible promoters and the like).

Recently issued U.S. Patent 6,692,962 discusses further details of this technology.

Because this technology affects cellular regulation, its applications are numerous, ranging from yield improvement (especially in grain quality and weight), to maturity control, to biomass elevation (for forages). Modification of the eIF2a phosphorylation pathway has further implications in the regulation of plant response to stress, virus and viroid infection and RNAi interactions. The use of inducible expression with this technology further increases potential commercial targets.

If you would like to learn more about this technology, or bring it in-house for evaluation or commercial uses, please contact the director of the Wyoming Research Products Center, Davona Douglass. We realize that today’s agricultural biotechnology companies have many choices when it comes to the evaluation of potential gene targets. The University of Wyoming is signing very reasonable research licenses for this technology so that its ultimate transfer to industry is as simplified and streamlined as possible. Please call for details.


Background References

Chang, Yang, Browning, Roth, “Specific in vitro phosphorylation of plant eIF2α by eukaryotic eIF2α kinases”, Plant Molecular Biology, 41: 363-370, 1999.

Gil, Esteban, Roth, “In vivo regulation of protein synthesis by phosphorylation of the α subunit of wheat eukaryotic initiation factor 2”, Biochemistry, Volume 39, Number 25, Pages 7521-7530.

Hiddinga, Crum, Hu, Roth, “Viroid-induced phosphorylation of a host protein related to a dsRNA-dependent protein kinase”, Science 22 July 1988, Volume 241, pp. 451-453.

Langland, Jin, Jacobs, Roth, “Identification of a plant-encoded analog of PKR, the mammalian double-stranded RNA-dependent protein kinase”, Plant Physiol. (1995) 108:1259-1267.

Langland, Landland, Browning, Roth, “Phosphorylation of plant eukaryotic initiation factor-2 by the plant-encoded double-stranded RNA-dependent protein kinase, pPKR, and inhibition of protein synthesis in vitro”, The Journal of Biological Chemistry, Vol 271, No. 8, Issue of February 23, pp. 4539-4544, 1996.

Roth, He, “Viral-dependent phosphorylation of a dsRNA-dependent kinase”, Progress in Molecular and Subcellular Biology, Vol. 14, W.E.G. Mueller/H.C. Schroeder (Eds.).