Identification of the amino acid residues responsible for cold tolerance in Flaveria brownii pyruvate,orthophosphate dikinase

FEBS Letters

Burnell, Jim N.²  Ueki, Jun¹  Komari, Toshihiko¹  Kumashiro, Takashi¹  Ohta, Shozo¹  Usami, Satoru¹ 

[1] Plant Breeding and Genetics Research Laboratory, Japan Tobacco Inc., 700 Higashibara, Toyoda, Iwata, Shizuoka, 438, Japan;Department of Biochemistry and Molecular Biology, James Cook University of North Queensland, Townsville, Qld. 4811, Australia

关键词: Pyruvate;    orthophosphate dikinase;    C4 photosynthesis;    Chilling;    Flaveria;   

DOI  :  10.1016/0014-5793(96)01084-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Pyruvate,orthophosphate dikinase (PPDK), an enzyme important in C₄ photosynthesis, is typically a cold-sensitive enzyme. However, a cold-tolerant form of the enzyme has been isolated from the leaves of Flaveria brownii. Using an Escherichia coli expression system and the PPDK cDNAs from F. brownii (cold-tolerant), F. bidentis (cold-sensitive) and maize (intermediate cold tolerance), site-directed mutagenesis studies indicated that as few as three amino acids residues (of 880 residues) strongly influence the cold sensitivity of Flaveria PPDK. Gel filtration analysis of the PPDK expressed in E. coli showed that subunit association and cold tolerance are closely linked.

【 授权许可】

Unknown