Journal Article

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

Tsuyoshi Furumoto, Maki Teramoto, Noriko Inada, Masaki Ito, Ikuo Nishida and Akira Watanabe

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 42, issue 10, pages 1044-1048
Published in print October 2001 | ISSN: 0032-0781
Published online October 2001 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pce161
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

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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.

Keywords: Key words: Arabidopsis thaliana — Carbon metabolism — Fructose 2,6-bisphosphate — 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase (EC 2.7.1.105/EC 3.1.3.46).; Abbreviations: CIP, calf intestine alkaline phosphatase; DTT, dithiothreitol; F2,6BP, fructose 2,6-bisphosphate; Fru-2,6-P2ase, fructose-2,6-bisphosphate 2-phosphatase; 6PF-2-K, 6-phosphofructo-2-kinase; PFP, pyrophosphate:fructose-6-phosphate 1-phosphotransferase; RACE, rapid amplification of cDNA ends.

Journal Article.  3603 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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