Functional analysis of protein phosphatase 2C in rice
2003
Yang, K. | Jeong, D.H. | An, G.
Protein phosphorylation and dephosphorylation are major regulatory mechanisms that cells use to transmit signals from their extracellular environment to the interior. Two structurally distinct groups of serine/threonine phosphatases are known: the PP1/PP2A family and the PP2C family. Here, we focus on the functions related to development and stress response. We have obtained six rice expressed sequence tag clones that contain the highly conserved KAPP catalytic domain. In addition, we have isolated three clones from a young panicle cDNA library by polymerase chain reaction using degenerate primers. RNA gel blot analysis showed that some of these genes are expressed constitutively, while others are preferentially expressed in certain tissue. We also present data on inducibility of genes to stresses such as cold, salt, and abscisic acid. The yeast two-hybrid system is being employed to find regulatory partners or substrates of the PP2C clones. Transgenic plants expressing the antisense constructs of the genes are being analyzed to determine the functional roles of the PP2C clones.
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