Functional Modeling Identifies Paralogous Solanesyl-diphosphate Synthases That Assemble the Side Chain of Plastoquinone-9 in Plastids

Authors

• Anna Block, University of Nebraska-LincolnFollow
• Rikard Fristedt, University of California, Los Angeles
• Sara Rogers, University of Nebraska-Lincoln
• Jyothi Kumar, University of Nebraska-LincolnFollow
• Brian Barnes, University of Nebraska- Lincoln
• Joshua Barnes, University of Nebraska-Lincoln
• Christian Elowsky, University of Nebraska-LincolnFollow
• Yashitola Wamboldt, University of Nebraska - LincolnFollow
• Sally Ann Mackenzie, University of Nebraska-LincolnFollow
• Kevin Redding, Arizona State University
• Sabeeha S. Merchant, University of California, Los Angeles
• Gilles J. Basset, University of Nebraska-LincolnFollow

ORCID IDs

Christian Elowsky

Document Type

Article

Date of this Version

2013

Citation

THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 288, NO. 38, pp. 27594–27606

Comments

© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

Abstract

Background: Plastid isoforms of solanesyl-diphosphate synthase catalyze the elongation of the prenyl side chain of plastoquinone-9.

Results: Corresponding mutants display lower levels of plastoquinone-9 and plastochromanol-8 and display intact levels of vitamin E.

Conclusion: Plastochromanol-8 originates from a subfraction of non-photoactive plastoquinol-9 and is not essential for seed longevity.

Significance: Viable plastoquinone-9 mutants are invaluable tools for understanding plastid metabolism.