Polyprenols Are Synthesized by a Plastidial cis-Prenyltransferase and Influence Photosynthetic Performance. Issue 7 (27th June 2017)
- Record Type:
- Journal Article
- Title:
- Polyprenols Are Synthesized by a Plastidial cis-Prenyltransferase and Influence Photosynthetic Performance. Issue 7 (27th June 2017)
- Main Title:
- Polyprenols Are Synthesized by a Plastidial cis-Prenyltransferase and Influence Photosynthetic Performance
- Authors:
- Akhtar, Tariq A.
Surowiecki, Przemysław
Siekierska, Hanna
Kania, Magdalena
Van Gelder, Kristen
Rea, Kevin A.
Virta, Lilia K.A.
Vatta, Maritza
Gawarecka, Katarzyna
Wojcik, Jacek
Danikiewicz, Witold
Buszewicz, Daniel
Swiezewska, Ewa
Surmacz, Liliana - Abstract:
- Abstract : A plastidial cis -prenyltransferase synthesizes a family of polyprenols that accumulate in thylakoid membranes and play a central role in the efficiency of photosynthetic performance. Abstract: Plants accumulate a family of hydrophobic polymers known as polyprenols, yet how they are synthesized, where they reside in the cell, and what role they serve is largely unknown. Using Arabidopsis thaliana as a model, we present evidence for the involvement of a plastidial cis -prenyltransferase (AtCPT7) in polyprenol synthesis. Gene inactivation and RNAi-mediated knockdown of AtCPT7 eliminated leaf polyprenols, while its overexpression increased their content. Complementation tests in the polyprenol-deficient yeast ∆rer2 mutant and enzyme assays with recombinant AtCPT7 confirmed that the enzyme synthesizes polyprenols of ∼55 carbons in length using geranylgeranyl diphosphate (GGPP ) and isopentenyl diphosphate as substrates. Immunodetection and in vivo localization of AtCPT7 fluorescent protein fusions showed that AtCPT7 resides in the stroma of mesophyll chloroplasts. The enzymatic products of AtCPT7 accumulate in thylakoid membranes, and in their absence, thylakoids adopt an increasingly "fluid membrane" state. Chlorophyll fluorescence measurements from the leaves of polyprenol-deficient plants revealed impaired photosystem II operating efficiency, and their thylakoids exhibited a decreased rate of electron transport. These results establish that (1) plastidial AtCPT7Abstract : A plastidial cis -prenyltransferase synthesizes a family of polyprenols that accumulate in thylakoid membranes and play a central role in the efficiency of photosynthetic performance. Abstract: Plants accumulate a family of hydrophobic polymers known as polyprenols, yet how they are synthesized, where they reside in the cell, and what role they serve is largely unknown. Using Arabidopsis thaliana as a model, we present evidence for the involvement of a plastidial cis -prenyltransferase (AtCPT7) in polyprenol synthesis. Gene inactivation and RNAi-mediated knockdown of AtCPT7 eliminated leaf polyprenols, while its overexpression increased their content. Complementation tests in the polyprenol-deficient yeast ∆rer2 mutant and enzyme assays with recombinant AtCPT7 confirmed that the enzyme synthesizes polyprenols of ∼55 carbons in length using geranylgeranyl diphosphate (GGPP ) and isopentenyl diphosphate as substrates. Immunodetection and in vivo localization of AtCPT7 fluorescent protein fusions showed that AtCPT7 resides in the stroma of mesophyll chloroplasts. The enzymatic products of AtCPT7 accumulate in thylakoid membranes, and in their absence, thylakoids adopt an increasingly "fluid membrane" state. Chlorophyll fluorescence measurements from the leaves of polyprenol-deficient plants revealed impaired photosystem II operating efficiency, and their thylakoids exhibited a decreased rate of electron transport. These results establish that (1) plastidial AtCPT7 extends the length of GGPP to ∼55 carbons, which then accumulate in thylakoid membranes; and (2) these polyprenols influence photosynthetic performance through their modulation of thylakoid membrane dynamics. … (more)
- Is Part Of:
- The Plant Cell. Volume 29:Issue 7(2017)
- Journal:
- The Plant Cell
- Issue:
- Volume 29:Issue 7(2017)
- Issue Display:
- Volume 29, Issue 7 (2017)
- Year:
- 2017
- Volume:
- 29
- Issue:
- 7
- Issue Sort Value:
- 2017-0029-0007-0000
- Page Start:
- 1709
- Page End:
- 1725
- Publication Date:
- 2017-06-27
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.16.00796 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16308.xml