Lack of Blue Light Regulation of Antioxidants and Chilling Tolerance in Basil

2021 ◽  
Author(s):  
Dorthe H. Larsen ◽  
Hua Li ◽  
Samikshya Shrestha ◽  
Julian C. Verdunk ◽  
Celine C.S. Nicole ◽  
...  
2011 ◽  
Vol 77 (4-5) ◽  
pp. 501-511 ◽  
Author(s):  
Qingyun Bu ◽  
Alicia Castillon ◽  
Fulu Chen ◽  
Ling Zhu ◽  
Enamul Huq

Trees ◽  
1999 ◽  
Vol 14 (3) ◽  
pp. 0169
Author(s):  
F. Rapparini ◽  
A. Rotondi ◽  
R. Baraldi
Keyword(s):  

Author(s):  
Didier Combes ◽  
Romain Barillot ◽  
Jean-Louis Durand ◽  
Abraham J. Escobar-Gutiérrez ◽  
Ela Frak

Biochemistry ◽  
2014 ◽  
Vol 53 (31) ◽  
pp. 5121-5130 ◽  
Author(s):  
Manuela Stierl ◽  
Alfons Penzkofer ◽  
John T. M. Kennis ◽  
Peter Hegemann ◽  
Tilo Mathes

2018 ◽  
Vol 56 (1) ◽  
pp. 41-66 ◽  
Author(s):  
Gwyn A. Beattie ◽  
Bridget M. Hatfield ◽  
Haili Dong ◽  
Regina S. McGrane

Plants collect, concentrate, and conduct light throughout their tissues, thus enhancing light availability to their resident microbes. This review explores the role of photosensing in the biology of plant-associated bacteria and fungi, including the molecular mechanisms of red-light sensing by phytochromes and blue-light sensing by LOV (light-oxygen-voltage) domain proteins in these microbes. Bacteriophytochromes function as major drivers of the bacterial transcriptome and mediate light-regulated suppression of virulence, motility, and conjugation in some phytopathogens and light-regulated induction of the photosynthetic apparatus in a stem-nodulating symbiont. Bacterial LOV proteins also influence light-mediated changes in both symbiotic and pathogenic phenotypes. Although red-light sensing by fungal phytopathogens is poorly understood, fungal LOV proteins contribute to blue-light regulation of traits, including asexual development and virulence. Collectively, these studies highlight that plant microbes have evolved to exploit light cues and that light sensing is often coupled with sensing other environmental signals.


2016 ◽  
Vol 113 (24) ◽  
pp. 6659-6664 ◽  
Author(s):  
Mio Ohki ◽  
Kanako Sugiyama ◽  
Fumihiro Kawai ◽  
Hitomi Tanaka ◽  
Yuuki Nihei ◽  
...  

Cyclic-AMP is one of the most important second messengers, regulating many crucial cellular events in both prokaryotes and eukaryotes, and precise spatial and temporal control of cAMP levels by light shows great promise as a simple means of manipulating and studying numerous cell pathways and processes. The photoactivated adenylate cyclase (PAC) from the photosynthetic cyanobacterium Oscillatoria acuminata (OaPAC) is a small homodimer eminently suitable for this task, requiring only a simple flavin chromophore within a blue light using flavin (BLUF) domain. These domains, one of the most studied types of biological photoreceptor, respond to blue light and either regulate the activity of an attached enzyme domain or change its affinity for a repressor protein. BLUF domains were discovered through studies of photo-induced movements of Euglena gracilis, a unicellular flagellate, and gene expression in the purple bacterium Rhodobacter sphaeroides, but the precise details of light activation remain unknown. Here, we describe crystal structures and the light regulation mechanism of the previously undescribed OaPAC, showing a central coiled coil transmits changes from the light-sensing domains to the active sites with minimal structural rearrangement. Site-directed mutants show residues essential for signal transduction over 45 Å across the protein. The use of the protein in living human cells is demonstrated with cAMP-dependent luciferase, showing a rapid and stable response to light over many hours and activation cycles. The structures determined in this study will assist future efforts to create artificial light-regulated control modules as part of a general optogenetic toolkit.


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