Plant & Animal Genomes XIII Conference

January 15-19, 2005
Town & Country Convention Center
San Diego, CA

Discovery Of Kinase-Associated Protein Phosphatase In Soybean

Akira Miyahara¹ , Artem E. Men² , Peter M. Gresshoff¹

¹  ARC Centre of Excellence for Integrative Legume Research, the University of Queensland, Brisbane, QLD 4072, Australia

²  ARGF, Brisbane, Australia

The Leguminosae such as soybean, pea and bean have the unique ability to interact with a bacterium called Rhizobium. As a result, legume plants are able to form nodules and fix atmospheric nitrogen. The nitrogen-fixing nodules respond to rhizobacteria via long-distance signaling known as autoregulation of nodulation (AON).
A receptor-like protein kinase (RLK), GmNARK (Glycine max nodule autoregulation receptor kinase) that controls AON has been isolated from soybean. This gene has high homology to one of well characterized RLKs, CLAVATA1 (CLV1), which plays an important role in the proper balance between cell proliferation and differentiation in Arabidopsis shoot apical and floral meristems. Kinase-associated protein phosphatase (KAPP) in vitro interacts with several plant RLKs including CLV1. Recent studies showed KAPP is a negative regulator in RLK signaling pathways. Here, in order to help understanding of the GmNARK signal transduction pathway, the soybean homolog of KAPP that encodes a kinase interaction domain and a type 2C protein phosphatase catalytic domain has been isolated.