scholarly journals Contrasting Responses of Photosynthesis to Salt Stress in the Glycophyte Arabidopsis and the Halophyte Thellungiella: Role of the Plastid Terminal Oxidase as an Alternative Electron Sink

2008 ◽  
Vol 149 (2) ◽  
pp. 1154-1165 ◽  
Author(s):  
Piotr Stepien ◽  
Giles N. Johnson
Authorea ◽  
2020 ◽  
Author(s):  
Jemaa Essemine ◽  
Ming Ju Amy Lyu ◽  
Mingnan Qu ◽  
Shahnaz Perveen ◽  
Naveed Khan ◽  
...  

2007 ◽  
Vol 145 (3) ◽  
pp. 691-702 ◽  
Author(s):  
Maryam Shahbazi ◽  
Matthias Gilbert ◽  
Anne-Marie Labouré ◽  
Marcel Kuntz

2020 ◽  
Vol 11 ◽  
Author(s):  
Jemaa Essemine ◽  
Ming-Ju Amy Lyu ◽  
Mingnan Qu ◽  
Shahnaz Perveen ◽  
Naveed Khan ◽  
...  

2017 ◽  
Vol 372 (1730) ◽  
pp. 20160379 ◽  
Author(s):  
Kathleen Feilke ◽  
Ghada Ajlani ◽  
Anja Krieger-Liszkay

Cyanobacteria are the most ancient organisms performing oxygenic photosynthesis, and they are the ancestors of plant plastids. All plastids contain the plastid terminal oxidase (PTOX), while only certain cyanobacteria contain PTOX. Many putative functions have been discussed for PTOX in higher plants including a photoprotective role during abiotic stresses like high light, salinity and extreme temperatures. Since PTOX oxidizes PQH 2 and reduces oxygen to water, it is thought to protect against photo-oxidative damage by removing excess electrons from the plastoquinone (PQ) pool. To investigate the role of PTOX we overexpressed rice PTOX fused to the maltose-binding protein (MBP-OsPTOX) in Synechocystis sp. PCC 6803, a model cyanobacterium that does not encode PTOX. The fusion was highly expressed and OsPTOX was active, as shown by chlorophyll fluorescence and P 700 absorption measurements. The presence of PTOX led to a highly oxidized state of the NAD(P)H/NAD(P) + pool, as detected by NAD(P)H fluorescence. Moreover, in the PTOX overexpressor the electron transport capacity of PSI relative to PSII was higher, indicating an alteration of the photosystem I (PSI) to photosystem II (PSII) stoichiometry. We suggest that PTOX controls the expression of responsive genes of the photosynthetic apparatus in a different way from the PQ/PQH 2 ratio. This article is part of the themed issue ‘Enhancing photosynthesis in crop plants: targets for improvement’.


AMB Express ◽  
2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Chunmiao Jiang ◽  
Gongbo Lv ◽  
Jinxin Ge ◽  
Bin He ◽  
Zhe Zhang ◽  
...  

AbstractGATA transcription factors (TFs) are involved in the regulation of growth processes and various environmental stresses. Although GATA TFs involved in abiotic stress in plants and some fungi have been analyzed, information regarding GATA TFs in Aspergillusoryzae is extremely poor. In this study, we identified and functionally characterized seven GATA proteins from A.oryzae 3.042 genome, including a novel AoSnf5 GATA TF with 20-residue between the Cys-X2-Cys motifs which was found in Aspergillus GATA TFs for the first time. Phylogenetic analysis indicated that these seven A. oryzae GATA TFs could be classified into six subgroups. Analysis of conserved motifs demonstrated that Aspergillus GATA TFs with similar motif compositions clustered in one subgroup, suggesting that they might possess similar genetic functions, further confirming the accuracy of the phylogenetic relationship. Furthermore, the expression patterns of seven A.oryzae GATA TFs under temperature and salt stresses indicated that A. oryzae GATA TFs were mainly responsive to high temperature and high salt stress. The protein–protein interaction network of A.oryzae GATA TFs revealed certain potentially interacting proteins. The comprehensive analysis of A. oryzae GATA TFs will be beneficial for understanding their biological function and evolutionary features and provide an important starting point to further understand the role of GATA TFs in the regulation of distinct environmental conditions in A.oryzae.


Author(s):  
Suhas Balasaheb Karle ◽  
Akankhya Guru ◽  
Padmanabh Dwivedi ◽  
Kundan Kumar
Keyword(s):  

2003 ◽  
Vol 270 (18) ◽  
pp. 3787-3794 ◽  
Author(s):  
Eve-Marie Josse ◽  
Jean-Pierre Alcaraz ◽  
Anne-Marie Laboure ◽  
Marcel Kuntz

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