Convergent evolution in the BAHD family of acyl transferases: identification and characterization of anthocyanin acyl transferases from Arabidopsis thaliana.
Members of the BAHD family of plant acyl transferases are very versatile catalytically, and are thought to be able to evolve new substrate specificities rapidly. Acylation of anthocyanins occurs in many plant species and affects anthocyanin stability and light absorption in solution. The versatility of BAHD acyl transferases makes it difficult to identify genes encoding enzymes with defined substrate specificities on the basis of structural homology to genes of known catalytic function alone. Consequently, we have used a modification to standard functional genomics strategies, incorporating co-expression profiling with anthocyanin accumulation, to identify genes encoding three anthocyanin acyl transferases from Arabidopsis thaliana. We show that the activities of these enzymes influence the stability of anthocyanins at neutral pH, and some acylations also affect the anthocyanin absorption maxima. These properties make the BAHD acyl transferases suitable tools for engineering anthocyanins for an improved range of biotechnological applications.
Luo
Jie
J
John Innes Centre, Norwich Research Park, Colney, Norwich, NR4 7UH, UK.
Nishiyama
Yasutaka
Y
Fuell
Christine
C
Taguchi
Goro
G
Elliott
Katherine
K
Hill
Lionel
L
Tanaka
Yoshikazu
Y
Kitayama
Masahiko
M
Yamazaki
Mami
M
Bailey
Paul
P
Parr
Adrian
A
Michael
Anthony J
AJ
Saito
Kazuki
K
Martin
Cathie
C
D000217:Acyltransferases / Q000235:genetics* / Q000378:metabolism; D000872:Anthocyanins / Q000378:metabolism*; D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D017931:DNA Primers; D019143:Evolution, Molecular; D017343:Genes, Plant; D006863:Hydrogen-Ion Concentration; D030821:Plants, Genetically Modified
D000872:Anthocyanins; D017931:DNA Primers; D000217:Acyltransferases