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Plant Physiol, October 1999, Vol. 121, pp. 609-618

The Arabidopsis Homolog of Yeast TAP42 and Mammalian alpha 4 Binds to the Catalytic Subunit of Protein Phosphatase 2A and Is Induced by Chilling1

Darby M. Harris, Tammy L. Myrick, and Sabine J. Rundle*

Department of Biology, Western Carolina University, Cullowhee, North Carolina 28723

Type 2A serine/threonine protein phosphatases (PP2A) have been implicated as important mediators of a number of plant growth and developmental processes. In an effort to identify plant PP2A substrates and/or regulators, we performed a yeast two-hybrid screen using an Arabidopsis PP2A catalytic subunit cDNA as bait. All true positives identified by this screen were derived from the same gene, which we have named TAP46 (2A phosphatase associated protein of 46 kD). The TAP46 gene appears to be a single-copy gene and is expressed in all Arabidopsis organs. Transcripts derived from this gene are induced by chilling treatment but not by heat or anaerobic stress. Immunoprecipitation assays using antibodies generated to a peptide spanning amino acids 356 to 366 of TAP46 indicate that TAP46 is associated with a type 2A protein phosphatase in vivo. A search of the database identified TAP46 as a homolog of Saccharomyces cerevisiae TAP42 and mammalian alpha 4. These two proteins are known to bind to the catalytic subunit of PP2A and to function in the target-of-rapamycin signaling pathway. Our results identify TAP46 as a plant PP2A-associated protein, with a possible function in the chilling response, and suggest that a target-of-rapamycin-like signaling pathway may exist in plants.

1 This work was supported by the U.S. Department of Agriculture (grant no. 96-35304-3863 to S.J.R.).

* Corresponding author; e-mail rundle{at}wpoff.wcu.edu; fax 828-227-7647.

© 1999 American Society of Plant Physiologists


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