scholarly journals The Functions of Chloroplast Glutamyl-tRNA in Translation and Tetrapyrrole Biosynthesis

2020 ◽  
Vol 183 (1) ◽  
pp. 263-276 ◽  
Author(s):  
Shreya Agrawal ◽  
Daniel Karcher ◽  
Stephanie Ruf ◽  
Ralph Bock
2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Daniel Wittmann ◽  
Neha Sinha ◽  
Bernhard Grimm

AbstractPlastids are specialized organelles found in plants, which are endowed with their own genomes, and differ in many respects from the intracellular compartments of organisms belonging to other kingdoms of life. They differentiate into diverse, plant organ-specific variants, and are perhaps the most versatile organelles known. Chloroplasts are the green plastids in the leaves and stems of plants, whose primary function is photosynthesis. In response to environmental changes, chloroplasts use several mechanisms to coordinate their photosynthetic activities with nuclear gene expression and other metabolic pathways. Here, we focus on a redox-based regulatory network composed of thioredoxins (TRX) and TRX-like proteins. Among multiple redox-controlled metabolic activities in chloroplasts, tetrapyrrole biosynthesis is particularly rich in TRX-dependent enzymes. This review summarizes the effects of plastid-localized reductants on several enzymes of this pathway, which have been shown to undergo dithiol-disulfide transitions. We describe the impact of TRX-dependent control on the activity, stability and interactions of these enzymes, and assess its contribution to the provision of adequate supplies of metabolic intermediates in the face of diurnal and more rapid and transient changes in light levels and other environmental factors.


2017 ◽  
Vol 175 (2) ◽  
pp. 652-666 ◽  
Author(s):  
Qingen Da ◽  
Peng Wang ◽  
Menglong Wang ◽  
Ting Sun ◽  
Honglei Jin ◽  
...  

FEBS Letters ◽  
2011 ◽  
Vol 586 (3) ◽  
pp. 211-216 ◽  
Author(s):  
Dominika Kauss ◽  
Sylvain Bischof ◽  
Sandro Steiner ◽  
Klaus Apel ◽  
Rasa Meskauskiene

Agronomy ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1370
Author(s):  
Dilrukshi S. K. Nagahatenna ◽  
Jingwen Tiong ◽  
Everard J. Edwards ◽  
Peter Langridge ◽  
Ryan Whitford

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 ~13% under controlled growth conditions now requires further research to determine if this can be translated to improved yield performance under field conditions.


1986 ◽  
Vol 146 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Rachel C. Hoult ◽  
Dyfrig Rees ◽  
Lyndon J. Rogers ◽  
Arnold J. Smith

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