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ARS Home » Research » Publications at this Location » Publication #185208


item Cooper, Bret
item Garrett, Wesley
item Campbell, Kimberly

Submitted to: Proteomics
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/30/2006
Publication Date: 5/30/2006
Citation: Cooper, B., Garrett, W.M., Campbell, K. 2006. Shotgun identification of proteins from uredospores of the bean rust uromyces appendiculatus. Proteomics. 6:2477-2484.

Interpretive Summary: Little is known about the proteins that make up the spores of fungi that cause rust diseases on beans. Knowledge of these proteins may lead to the discovery of chemicals that could inhibit germination of spores and the infection of plants. Mass spectrometry was used to identify proteins from rust spores. A majority of the proteins were heat-shock proteins, translation elongation factors and other proteins. Novel proteins were also discovered and these proteins may be unique targets for chemical inhibition. The results suggest that an abundance of heat-shock proteins, translation elongation factors and other protein making machinery enable the spores to jump-start protein production upon germination and withstand environmental temperature extremes. These abilities likely help improve a spore's ability to survive and infect plants. These data will be of use to scientists at universities, government agencies and companies who are designing new fungicides to fight rust diseases.

Technical Abstract: We are interested in learning more about the proteome of Uromyces appendiculatus, the fungus that causes common bean rust. Knowledge of the proteins that differentiate life cycle stages and distinguish infectious bodies such as uredospores, germlings, appressoria, and haustoria may be used to define host-pathogen interactions or serve as targets for chemical inhibition of the fungus. We have used two-dimensional nanoflow liquid chromatography tandem mass spectrometry (nanoLC-LC-MS/MS) to identify more than 400 proteins from asexual uredospores. A majority of the proteins appear to have roles in protein folding or protein catabolism. We present a model by which an abundance of heat-shock proteins and translation elongation factors enhances a spores ability to survive environmental stresses and rapidly initiate protein production upon germination.