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Characterization of homogentisate prenyltransferases involved in plastoquinone‐9 and tocochromanol biosynthesis
Author(s) -
Sadre Radin,
Gruber Jens,
Frentzen Margrit
Publication year - 2006
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/j.febslet.2006.09.002
Subject(s) - chlamydomonas reinhardtii , prenyltransferase , arabidopsis thaliana , plastoquinone , biosynthesis , biochemistry , biology , enzyme , chloroplast , chemistry , gene , thylakoid , mutant
A cDNA of Chlamydomonas reinhardtii encoding a plastidial homogentisate prenyltransferase was identified. Functional expression studies in Escherichia coli revealed that the enzyme possessed properties similar to the prenyltransferase of Arabidopsis thaliana encoded by At3g11950 but different from the phytyltransferases of A. thaliana and Synechocystis . Unlike the phytyltransferases, the C. reinhardtii and the respective A. thaliana enzyme showed highest activities with solanesyl diphosphate, but were hardly active with phytyl diphosphate. Hence, these data provide evidence that the latter represent homogentisate solanesyltransferases involved in plastoquinone‐9 biosynthesis. Overexpression of At3g11950 in A. thaliana , however, suggests that the solanesyltransferase can affect tocopherol biosynthesis as well.