Non-redox protein interactions in the thioredoxin activation of chloroplast enzymes.
Thioredoxin derivatives lacking SH groups such as S,S'-dicarboxymethyl-, dicarboxamidomethyl-thioredoxin and cysteine----serine mutant protein are capable of activating chloroplast NADP malate dehydrogenase and fructose-bisphosphatase when added to enzyme assays together with suboptimal amounts of native thioredoxin. The modified thioredoxins alone are inactive. These findings indicate that protein-protein interactions play a significant role in addition to disulfide/thiol exchange reactions in the light-driven regulation of plant enzymes by the various plant thioredoxins.
Häberlein
I
I
Fachbereich Biologie-Chemie, Biochemie, Universität Kassel, Germany.
Würfel
M
M
Follmann
H
H
D000595:Amino Acid Sequence; D002736:Chloroplasts / Q000201:enzymology*; D004789:Enzyme Activation; D004926:Escherichia coli / Q000378:metabolism; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000378:metabolism*; D050538:Malate Dehydrogenase (NADP+); D008969:Molecular Sequence Data; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013879:Thioredoxins / Q000378:metabolism*
D013438:Sulfhydryl Compounds; D013879:Thioredoxins; D009249:NADP; D008291:Malate Dehydrogenase; D050538:Malate Dehydrogenase (NADP+); D006597:Fructose-Bisphosphatase