Journal
PLANT JOURNAL
Volume 68, Issue 6, Pages 1051-1060Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1365-313X.2011.04756.x
Keywords
domain loss; evolution; metabolism; natural products; terpene synthases
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Funding
- Key Project of Chinese National Programs for Fundamental Research and Development (973 Program) [2006CB-504700]
- Chinese National Programs for High Technology Research and Development (863 Program) [2007AA02Z104]
- Japan Society for the Promotion of Science
- NIH [GM076324]
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The extensive family of plant terpene synthases (TPSs) generally has a bi-domain structure, yet phylogenetic analyses consistently indicate that these synthases have evolved from larger diterpene synthases. In particular, that duplication of the diterpene synthase genes required for gibberellin phytohormone biosynthesis provided an early predecessor, whose loss of a approximately 220 amino acid internal sequence element (now recognized as the ? domain) gave rise to the precursor of the modern mono- and sesqui-TPSs found in all higher plants. Intriguingly, TPSs are conserved by taxonomic relationships rather than function. This relationship demonstrates that such functional radiation has occurred both repeatedly and relatively recently, yet phylogenetic analyses assume that the internal/? domain loss represents a single evolutionary event. Here we provide evidence that such a loss was not a singular event, but rather has occurred multiple times. Specifically, we provide an example of a bi-domain diterpene synthase from Salvia miltiorrhiza, along with a sesquiterpene synthase from Triticum aestivum (wheat) that is not only closely related to diterpene synthases, but retains the ent-kaurene synthase activity relevant to the ancestral gibberellin metabolic function. Indeed, while the wheat sesquiterpene synthase clearly no longer contains the internal/? domain, it is closely related to rice diterpene synthase genes that retain the ancestral tri-domain structure. Thus, these findings provide examples of key evolutionary intermediates that underlie the bi-domain structure observed in the expansive plant TPS gene family, as well as indicating that internal/? domain loss has occurred independently multiple times, highlighting the complex evolutionary history of this important enzymatic family.
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