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Journal article
Altering Tetrapyrrole Biosynthesis by Overexpressing Ferrochelatases (Fc1 and Fc2) Improves Photosynthetic Efficiency in Transgenic Barley
Agronomy (Basel), Vol.10(9), 1370
2020
Abstract
Ferrochelatase (FC) is the terminal enzyme of heme biosynthesis. In photosynthetic organisms studied so far, there is evidence for two FC isoforms, which are encoded by two genes (FC1 and FC2). Previous studies suggest that these two genes are required for the production of two physiologically distinct heme pools with only FC2-derived heme involved in photosynthesis. We characterised two FCs in barley (Hordeum vulgare L.). The two HvFC isoforms share a common catalytic domain, but HvFC2 additionally contains a C-terminal chlorophyll a/b binding (CAB) domain. Both HvFCs are highly expressed in photosynthetic tissues, with HvFC1 transcripts also being abundant in non-photosynthetic tissues. To determine whether these isoforms differentially affect photosynthesis, transgenic barley ectopically overexpressing HvFC1 and HvFC2 were generated and evaluated for photosynthetic performance. In each case, transgenics exhibited improved photosynthetic rate (Asat), stomatal conductance (gs) and carboxylation efficiency (CE), showing that both FC1 and FC2 play important roles in photosynthesis. Our finding that modified FC expression can improve photosynthesis up to similar to 13% under controlled growth conditions now requires further research to determine if this can be translated to improved yield performance under field conditions.
Details
- Title
- Altering Tetrapyrrole Biosynthesis by Overexpressing Ferrochelatases (Fc1 and Fc2) Improves Photosynthetic Efficiency in Transgenic Barley
- Authors/Creators
- Dilrukshi S. K. Nagahatenna - The University of AdelaideJingwen Tiong - The University of AdelaideEverard J. Edwards - Commonwealth Scientific and Industrial Research OrganisationPeter Langridge - The University of AdelaideRyan Whitford - The University of Adelaide
- Publication Details
- Agronomy (Basel), Vol.10(9), 1370
- Publisher
- MDPI
- Number of pages
- 15
- Identifiers
- 991005779529807891
- Copyright
- © 2020 by the authors.
- Murdoch Affiliation
- Centre for Crop and Food Innovation
- Language
- English
- Resource Type
- Journal article
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InCites Highlights
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- Collaboration types
- Domestic collaboration
- International collaboration
- Citation topics
- 3 Agriculture, Environment & Ecology
- 3.171 Photoproductivity
- 3.171.129 Photosynthesis Mechanisms
- Web Of Science research areas
- Agronomy
- Plant Sciences
- ESI research areas
- Agricultural Sciences