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Keywords = NADH dehydrogenase-like complex (NDH)

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14 pages, 3360 KiB  
Article
OTP970 Is Required for RNA Editing of Chloroplast ndhB Transcripts in Arabidopsis thaliana
by Mei Fu, Xiaona Lin, Yining Zhou, Chunmei Zhang, Bing Liu, Dongru Feng, Jinfa Wang, Hongbin Wang and Honglei Jin
Genes 2022, 13(1), 139; https://doi.org/10.3390/genes13010139 - 14 Jan 2022
Cited by 3 | Viewed by 2882
Abstract
RNA editing is essential for compensating for defects or mutations in haploid organelle genomes and is regulated by numerous trans-factors. Pentatricopeptide repeat (PPR) proteins are the prime factors that are involved in RNA editing; however, many have not yet been identified. Here, [...] Read more.
RNA editing is essential for compensating for defects or mutations in haploid organelle genomes and is regulated by numerous trans-factors. Pentatricopeptide repeat (PPR) proteins are the prime factors that are involved in RNA editing; however, many have not yet been identified. Here, we screened the plastid-targeted PLS-DYW subfamily of PPR proteins belonging to Arabidopsis thaliana and identified ORGANELLE TRANSCRIPT PROCESSING 970 (OTP970) as a key player in RNA editing in plastids. A loss-of-function otp970 mutant was impaired in RNA editing of ndhB transcripts at site 149 (ndhB-C149). RNA-immunoprecipitation analysis indicated that OTP970 was associated with the ndhB-C149 site. The complementation of the otp970 mutant with OTP970 lacking the DYW domain (OTP970∆DYW) failed to restore the RNA editing of ndhB-C149. ndhB gene encodes the B subunit of the NADH dehydrogenase-like (NDH) complex; however, neither NDH activity and stability nor NDH-PSI supercomplex formation were affected in otp970 mutant compared to the wild type, indicating that alteration in amino acid sequence is not necessary for NdhB function. Together, these results suggest that OTP970 is involved in the RNA editing of ndhB-C149 and that the DYW domain is essential for its function. Full article
(This article belongs to the Special Issue Advances in Evolution of Plant Organelle Genome)
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19 pages, 19685 KiB  
Article
CAF Proteins Help SOT1 Regulate the Stability of Chloroplast ndhA Transcripts
by Xiuming Li, Wenzhen Luo, Wen Zhou, Xiaopeng Yin, Xuemei Wang, Xiujin Li, Chenchen Jiang, Qingqing Zhang, Xiaojing Kang, Aihong Zhang, Yi Zhang and Congming Lu
Int. J. Mol. Sci. 2021, 22(23), 12639; https://doi.org/10.3390/ijms222312639 - 23 Nov 2021
Cited by 6 | Viewed by 2344
Abstract
Protein-mediated RNA stabilization plays profound roles in chloroplast gene expression. Genetic studies have indicated that chloroplast ndhA transcripts, encoding a key subunit of the NADH dehydrogenase-like complex that mediates photosystem I cyclic electron transport and facilitates chlororespiration, are stabilized by PPR53 and its [...] Read more.
Protein-mediated RNA stabilization plays profound roles in chloroplast gene expression. Genetic studies have indicated that chloroplast ndhA transcripts, encoding a key subunit of the NADH dehydrogenase-like complex that mediates photosystem I cyclic electron transport and facilitates chlororespiration, are stabilized by PPR53 and its orthologs, but the underlying mechanisms are unclear. Here, we report that CHLOROPLAST RNA SPLICING 2 (CRS2)-ASSOCIATED FACTOR (CAF) proteins activate SUPPRESSOR OF THYLAKOID FORMATION 1 (SOT1), an ortholog of PPR53 in Arabidopsis thaliana, enhancing their affinity for the 5′ ends of ndhA transcripts to stabilize these molecules while inhibiting the RNA endonuclease activity of the SOT1 C-terminal SMR domain. In addition, we established that SOT1 improves the splicing efficiency of ndhA by facilitating the association of CAF2 with the ndhA intron, which may be due to the SOT1-mediated stability of the ndhA transcripts. Our findings shed light on the importance of PPR protein interaction partners in moderating RNA metabolism. Full article
(This article belongs to the Special Issue Post-transcriptional Regulation in Plant Organelles)
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17 pages, 1505 KiB  
Review
Current Knowledge on Mechanisms Preventing Photosynthesis Redox Imbalance in Plants
by María-Cruz González, Francisco Javier Cejudo, Mariam Sahrawy and Antonio Jesús Serrato
Antioxidants 2021, 10(11), 1789; https://doi.org/10.3390/antiox10111789 - 9 Nov 2021
Cited by 14 | Viewed by 4500
Abstract
Photosynthesis includes a set of redox reactions that are the source of reducing power and energy for the assimilation of inorganic carbon, nitrogen and sulphur, thus generating organic compounds, and oxygen, which supports life on Earth. As sessile organisms, plants have to face [...] Read more.
Photosynthesis includes a set of redox reactions that are the source of reducing power and energy for the assimilation of inorganic carbon, nitrogen and sulphur, thus generating organic compounds, and oxygen, which supports life on Earth. As sessile organisms, plants have to face continuous changes in environmental conditions and need to adjust the photosynthetic electron transport to prevent the accumulation of damaging oxygen by-products. The balance between photosynthetic cyclic and linear electron flows allows for the maintenance of a proper NADPH/ATP ratio that is adapted to the plant’s needs. In addition, different mechanisms to dissipate excess energy operate in plants to protect and optimise photosynthesis under adverse conditions. Recent reports show an important role of redox-based dithiol–disulphide interchanges, mediated both by classical and atypical chloroplast thioredoxins (TRXs), in the control of these photoprotective mechanisms. Moreover, membrane-anchored TRX-like proteins, such as HCF164, which transfer electrons from stromal TRXs to the thylakoid lumen, play a key role in the regulation of lumenal targets depending on the stromal redox poise. Interestingly, not all photoprotective players were reported to be under the control of TRXs. In this review, we discuss recent findings regarding the mechanisms that allow an appropriate electron flux to avoid the detrimental consequences of photosynthesis redox imbalances. Full article
(This article belongs to the Special Issue Redox in Plants)
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