Wisconsin Alumni Research Foundation

Richard David Vierstra

Andrew T Ulijasz

Junrui Zhang

Robert Joseph Stankey

Katrina T Forest

Judy Callis

Mark Mattnew Gosink

David Anstrom

David Hondred

Jeremiah R Wagner

Joseph M Walker

Polynucleotides encoding polypeptides that increase the light sensitivity of plants were identified. Introduction of the polynucleotides into plants produces plants having altered characteristics, such as decreased height, decreased diameter, decreased petiole length, decreased internode length, decreased hypocotyl length, increased hyponasty or enhanced germination.

Plants with altered phytochromes

Genetically-engineered cyanochrome fluorophore molecules (fluorophores) with increased fluorescence and with absorbing fluorescence in the blue and green (blue/green) portion of the light spectrum are provided. These fluorophores are derived from the domains of phytochromes, and in particular cyanobacterial phytochromes. Methods for generating these fluorophores and various applications of these fluorophores are also provided.

Cyanochrome fluorophores

Genetically-engineered fluorophore molecules with increased fluorescence are provided. These fluorophores are derived from the domains of phytochromes, and in particular bacterial phytochromes. Methods for generating these fluorophores and various applications of these fluorophores are also provided.

Phytochrome-based fluorophores

A method is disclosed for the production of multiple proteins in transgenic plants. A DNA construct for introduction into plants includes a provision to express a fusion protein of two proteins of interest joined by a linking domain including plant ubiquitin. When the fusion protein is produced in the cells of a transgenic plant transformed with the DNA construction, native enzymes present in plant cells cleave the fusion protein to release both proteins of interest into the cells of the transgenic plant. Since the proteins are produced from the same fusion protein, the initial quantities of the proteins in the cells of the plant are approximately equal.

Expression of multiple proteins in transgenic plants

A novel class of fusion proteins based on the ubiquitin-conjugating enzyme, or E2, is described. The fusion proteins include, in addition to the E2 activity, a protein binding ligand having a specific affinity for a target protein. It has been discovered that under cytosolic conditions, such E2 fusions will add a ubiquitin moiety to a target protein. Since ubiquitin addition triggers the endogenous cellular protein degradation pathway, such E2 fusion proteins can be used to selectively target proteins in a host for degradation. Thus, E2 fusion proteins genes can be introduced into transgenic organisms to defeat or inhibit natural activities or traits. The E2 fusion proteins can also be used by introduction into hosts for similar effects.

Ubiquitin conjugating enzyme (E2) fusion proteins

Ubiquitin is an abundantly expressed protein in all eukaryotic organisms. A gene for plant ubiquitin, isolated from Arabidopsis thaliana, has been used in a plant expression vector to produce a ubiquitin-protein fusion. Natural factors in the plant cleave such a fusion protein to release ubiquitin and the desired protein. It has been found that such fusions result in protein expression levels higher than those that can be obtained from expression of the protein alone.

Growing community of inventors

Madison, WI, United States of America

Richard David Vierstra