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ARS Home » Pacific West Area » Maricopa, Arizona » U.S. Arid Land Agricultural Research Center » Plant Physiology and Genetics Research » Research » Publications at this Location » Publication #204771
Title: Do maise and wheat chloroplast protein synthesis elongation factor, EF-Tu, protect Rubisco activase from thermal aggregation and inactivation?

Author
item MOMCILOVIC, IVANA - KANSAS STATE UNIV
item FU, JIANMING - KANSAS STATE UNIV
item BUKOVNIK, URSKA - KANSAS STATE UNIV
item Deridder, Benjamin
item Salvucci, Michael
item Ristic, Zoran

Submitted to: American Society of Plant Biologists
Publication Type: Abstract Only
Publication Acceptance Date: 8/4/2006
Publication Date: 8/9/2006
Citation: Momcilovic, I., Fu, J., Bukovnik, U., Deridder, B.P., Salvucci, M.E., Ristic, Z. 2006. Do maise and wheat chloroplast protein synthesis elongation factor, EF-Tu, protect Rubisco activase from thermal aggregation and inactivation?. American Society of Plant Biologists. Abstract # P09035. Available: http://abstracts.aspb.org/pb2006/public/cgi-bin/search.cgi.

Interpretive Summary:

Technical Abstract: Maize (Zea mays L.) chloroplast protein synthesis elongation factor, EF-Tu, has been implicated in the development of heat tolerance. The precursor of this protein (pre-EF-Tu) has been shown to display chaperone activity, as it protected heat labile citrate synthase and malate dehydrogenase from thermal aggregation and inactivation [Eur. J. Biochem. (2004) 271: 3684-3692]. In the present study, we tested the chaperone activity of maize recombinant pre-EF-Tu towards recombinant maize and wheat (Triticum aestivum L.) Rubisco activase. In addition, we also tested the possible chaperone activity of native maize and wheat EF-Tu using recombinant activase from maize and wheat as a substrate. The recombinant proteins (pre-EF-Tu and Rubisco activase) were purified from E. coli, and the native EF-Tu was purified from maize/wheat leaf tissue. Chaperone assays were conducted in vitro. The results showed that recombinant maize pre-EF-Tu protected activase from heat-induced aggregation. Preliminary results showed that native EF-Tu also displays chaperone activity towards activase. Wheat EF-Tu, for instance, prevented thermal aggregation of maize activase in a concentration dependent manner. Further studies are in progress to determine whether EF-Tu protects Rubisco activase from thermal inactivation.