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ARS Home » Plains Area » Fargo, North Dakota » Edward T. Schafer Agricultural Research Center » Cereal Crops Research » Research » Publications at this Location » Publication #207637

Title: Interactome of Signaling Networks in Wheat: the Protein-Protein Interaction between TaRAR1 and TaSCT1

Author
item Tai, Yin Shan

Submitted to: Molecular Biology Reports
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 4/30/2007
Publication Date: N/A
Citation: N/A

Interpretive Summary: Proteins in plant cells interact in networks like the highways on a map. Many functions important for cell development and survival are mediated by protein-protein interactions. Wheat disease resistance against leaf rust requires a protein known as Lr21, which is the first NBS-LRR-type resistance (R) gene identified in wheat (resistance genes are classified into different types). NBS-LRR-type R genes, which encode proteins with nucleotide-binding-site (NBS) and leucine-rich-repeat (LRR) domains, are the most prevalent resistance genes in plants. The signaling pathways of Lr21-mediated resistance involve three components identified to date: TaRAR1, TaSGT1, and TaHSP90. However, the molecular mechanism underlying how these components regulate resistance is not known. This report demonstrates a protein-protein interaction between TaRAR1 and TaSGT1. This will help pave the way to understanding the molecular mechanism of wheat resistance to leaf rust. The long-term goal for this study is to understand the Lr21-mediated protein-protein networks (or the so-called interactome).

Technical Abstract: RAR1 and SGT1 are required for development and disease resistance. In many cases, RAR1 and SGT1 regulate the resistance (R)-gene-mediated defense signaling pathways. Lr21 is the first identified NBS-LRR-type R protein in wheat and is required for resistance to the fungal pathogen of leaf rust disease. The Lr21-mediated signaling pathways require the wheat homologs of RAR1, SGT1, and HSP90. However, the molecular links of the Lr21-mediated signaling networks remain unknown. Here I present the DNA and protein sequences of TaRAR1 and TaSGT1. For the first report in wheat, I demonstrate the direct protein-protein interaction between TaRAR1 and TaSGT1.