Richard Vierstra

Richard Vierstra
Professor

Ph.D., Michigan State University, 1980
Postdoctoral Research: University of Wisconsin-Madison 

Address: 3104 Genetics/Biotech

Telephone: 608-262-8215

E-mail:

Department: Genetics

Research Interests

Dissect the pathways used to remove regulatory proteins and unwanted cellular constituents and direct light perception and photomorphogenesis in plants

Research Fields

Cell Biology
Development
Evolutionary & Population Genetics
Genomics & Proteomics
Bacteria
Plants

Research Description:

Our laboratory is attempting to elucidate the molecular mechanisms used by eukaryotes to selectively degrade intracellular proteins. Protein degradation has an integral role in cell maintenance, growth, and development and is an important component in the ability to genetically engineer organisms. Three fundamental questions are: (i) What are the pathways used to breakdown proteins and how are they selective? (ii) What specific functions does proteolysis have in cell physiology? And (iii) how can proteolysis be beneficially manipulated? One pathway of interest involves the conserved protein ubiquitin. It functions by becoming covalently attached to proteins targeted for catabolism, and then serves as a reusable recognition signal for target breakdown by the multisubunit 26S proteasome. We are studying this pathway by various approaches with special emphasis on the model plant, Arabidopsis thaliana. Of interest is a characterization of components involved in ubiquitin conjugation and an understanding of how these factors choose appropriate substrates. By reverse genetic methods, we are generating a wide array of mutants that should reveal the pathway’s function in Arabidopsis growth and development. As a model for selective proteolysis, we are also studying the form-dependent degradation of the morphogenic photoreceptor, phytochrome. This protein is unique in that its in vivo degradation rate by the ubiquitin pathway can be altered over 100 fold simply by illuminating plants with light. 

Representative Publications:

Search PubMed for more publications by Richard Vierstra

Wagner, J.R., Brunzelle, J.S., Forest, K.T. and Vierstra, R.D. 2005. A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome. Nature. 438:325-331. 

Gingerich, D.J., Gagne, J.M., Helleman, H., Estelle, M., Ma, L. and R.D. Vierstra. 2005. Cullin 3A and B assemble with members of the broad complex/tramtrack/bric-a-brac (BTB) protein family to form essential ubiquitin-protein ligases in Arabidopsis. J. Biol Chem. 280:18810-18821. 

Thompson, A.R., Doelling, J.H., Suttangkakul, A. and R.D. Vierstra. 2005. Autophagic nutrient recycling in Arabidopsis thaliana directed by the ATG8 and ATG12 conjugation pathways. Plant Physiol. 138:2097-2110. 

Gagne, J.M., Smalle, J., Gingerich, D.J., Walker, J.M., Yoo, S.-D., Yanagisawa, S. and Vierstra, R.D. 2004. Arabidopsis EIN3-binding F-box 1 and 2 form ubiquitin-protein ligases that repress ethylene action and promote growth by directing EIN3 degradation. Proc. Natl. Acad. Sci. USA 101:6803-6808.

Smalle, J. and Vierstra, R.D. 2004. The ubiquitin 26S proteasome proteolytic pathway. Ann. Rev. Plant Biol. 55:555-590. 

Downes, B.P., Stupar, R.M., Gingerich, D.J., and Vierstra, R.D. 2003. The HECT ubiquitin-protein ligase family in Arabidopsis: UPL3 has a specific role in trichome development. Plant J. 35:729-742. 

Karniol, B. and Vierstra, R.D. 2004. The HWE histidine kinases, a new family of bacterial two-component sensor kinases with potentially diverse roles in environmental signaling. J. Bactertiol. 186:445-453. 

Davis, S.J., J. Kurepa, and R.D. Vierstra. 1999. The Arabidopsis thaliana HY1 locus, required for phytochrome chromophore biosynthesis, encodes a protein related to heme oxygenases. Proc. Natl. Acad. Sci. USA. 96:6541-6546. 

Davis, S.J., A. Vener, and R.D. Vierstra. 1999. Bacteriophytochromes, phytochrome-like photoreceptors from non-photosynthetic eubacteria. Science 286:2517-2520. 

Vierstra, R.D., and J. Callis. 1999 Polypeptide tags, ubiquitous modifiers for plant protein regulation. Plant Mol. Biol. 41:435-442.