A new o-methyltransferase for monolignol synthesis in carthamus tinctorius

1Citations
Citations of this article
14Readers
Mendeley users who have this article in their library.

Abstract

A novel type of O-methyltransferase (OMT) cDNA was isolated from maturing seeds of Carthamus tinctorius (safflower). The deduced sequence of the OMT protein showed moderate sequence identity (52%) with C. tinctorius 5-hydroxyconiferaldehyde O-methyltransferase 1 (CAldOMT1). Phylogenetic analysis showed that the novel OMT did not belong to the typical CAldOMT [=caffeic acid OMT (CAOMT)] cluster. The recombinant protein of the OMT catalyzed 3-(or 5-) O-methylation of hydroxycinnamaldehydes and hydroxycinnamyl alcohols, while it showed only weak or moderate activity toward hydroxycinnamates and hydroxycinnamoyl coenzyme A esters. Therefore, this OMT was designated as C. tinctorius 5-hydroxyconiferaldehyde/5-hydroxyconiferyl alcohol OMT (CtAAOMT). The time profile of CtAAOMT gene expression in C. tinctorius matched the patterns of lignin accumulation. Taken together, our data strongly suggest that along with CtCAldOMT1, CtAAOMT is involved in biosynthesis of syringyl lignin.

Cite

CITATION STYLE

APA

Nakatsubo, T., Ragamustari, S. K., Hattori, T., Ono, E., Yamamura, M., Li, L., … Umezawa, T. (2014). A new o-methyltransferase for monolignol synthesis in carthamus tinctorius. Plant Biotechnology, 31(5), 545–553. https://doi.org/10.5511/plantbiotechnology.14.0903a

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free