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Plant and Cell Physiology, 2001, Vol. 42, No. 10 1044-1048
© 2001 Oxford University Press

Phosphorylation of a Bifunctional Enzyme, 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase, is Regulated Physiologically and Developmentally in Rosette Leaves of Arabidopsis thaliana

Tsuyoshi Furumoto1,2, Maki Teramoto3, Noriko Inada, Masaki Ito, Ikuo Nishida and Akira Watanabe4

Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, 113-0033 Japan

The phosphorylation status of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase (EC 2.7.1.105/ EC 3.1.3.46) in rosette leaves of Arabidopsis was examined. Immunoblotting with specific antisera detected 96-kDa and 92-kDa bands in the crude protein extracts from rosette leaves of Arabidopsis. Incubation of protein samples with alkaline phosphatase before SDS-PAGE reduced the 96-kDa band with concomitant increase of the 92-kDa band, suggesting that the former is a phosphorylated form of the latter. In accordance with this result, 96-kDa and 92-kDa bands were immuno-precipitated from the crude protein extracts from [32P]orthophosphate-labeled rosettes of Arabidopsis; and, the former was heavily labeled, the latter faintly labeled. Analysis of phospho-amino acid residues derived from the [32P]-labeled 96-kDa band revealed that the phosphorylation occurred on serine and threonine residues, excluding the possibility that the phosphorylated band represent a phospho-histidine intermediate that is known to form in the phosphatase reaction. The relative level of the 96-kDa band over the 92-kDa band in whole rosette extracts changed diurnally and was highest at the beginning of nighttime. Furthermore, the 96-kDa band was highly enriched in the extracts of very young rosette leaves, suggesting that the phosphorylation status of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase is regulated physiologically and developmentally in Arabidopsis.

1 Corresponding author: E-mail, furumoto@lif.kyoto-u.ac.jp; Fax, +81-75-753-6470.

2 Present address: Laboratory of Plant Physiology, Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto, 606-8502 Japan.

3 Present address: Marine Biotechnology Institute, Kamaishi Laboratories, 3-75-1 Heita, Kamaishi, Iwate, 026-0001 Japan.

4 Deceased on May 22, 2000.


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