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Identification of the amino acid residues responsible for cold tolerance in Flaveria brownii pyruvate,orthophosphate dikinase
Author(s) -
Ohta Shozo,
Usami Satoru,
Ueki Jun,
Kumashiro Takashi,
Komari Toshihiko,
Burnell Jim N.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01084-8
Subject(s) - biochemistry , cold sensitivity , enzyme , photosynthesis , amino acid , phosphoenolpyruvate carboxykinase , biology , chemistry , protein subunit , mutagenesis , gene , mutation , mutant
Pyruvate,orthophosphate dikinase (PPDK), an enzyme important in C 4 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.