CBF-Dependent Cold Stress Signaling Relevant Post Translational Modifications

2013 ◽  
pp. 105-122 ◽  
Author(s):  
Prakriti Kashyap ◽  
Renu Deswal
Keyword(s):  
Cold Stress ◽  
Stress Signaling ◽  
Post Translational Modifications

scholarly journals Response to the Cold Stress Signaling of the Tea Plant (Camellia sinensis) Elicited by Chitosan Oligosaccharide

Agronomy ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 915 ◽  
Author(s):  
Yingying Li ◽  
Qiuqiu Zhang ◽  
Lina Ou ◽  
Dezhong Ji ◽  
Tao Liu ◽  
...  
Keyword(s):  
Low Temperature ◽  
Cold Stress ◽  
Soluble Sugar ◽  
Tea Plant ◽  
Chitosan Oligosaccharide ◽  
Stress Signaling ◽  
Molecular Response ◽  
Tea Leaves ◽  
Sod Activity ◽  
Tea Plants

Cold stress caused by a low temperature is a significant threat to tea production. The application of chitosan oligosaccharide (COS) can alleviate the effect of low temperature stress on tea plants. However, how COS affects the cold stress signaling in tea plants is still unclear. In this study, we investigated the level of physiological indicators in tea leaves treated with COS, and then the molecular response to the cold stress of tea leaves treated with COS was analyzed by transcriptomics with RNA-Sequencing (RNA-Seq). The results show that the activity of superoxide dismutase (SOD) activity, peroxidase (POD) activity, content of chlorophyll and soluble sugar in tea leaves in COS-treated tea plant were significantly increased and that photosynthesis and carbon metabolism were enriched. Besides, our results suggest that COS may impact to the cold stress signaling via enhancing the photosynthesis and carbon process. Our research provides valuable information for the mechanisms of COS application in tea plants under cold stress.

Cold stress signaling networks in Arabidopsis

2013 ◽  
Vol 56 (2) ◽  
pp. 69-76 ◽  
Author(s):  
Jin Jeon ◽  
Jungmook Kim
Keyword(s):  
Cold Stress ◽  
Signaling Networks ◽  
Stress Signaling

scholarly journals Disruption of Arabidopsis CHY1 Reveals an Important Role of Metabolic Status in Plant Cold Stress Signaling

2009 ◽  
Vol 2 (1) ◽  
pp. 59-72 ◽  
Author(s):  
Chun-Hai Dong ◽  
Bethany K. Zolman ◽  
Bonnie Bartel ◽  
Byeong-ha Lee ◽  
Becky Stevenson ◽  
...  
Keyword(s):  
Cold Stress ◽  
Metabolic Status ◽  
Stress Signaling

scholarly journals Convergence and Divergence: Signal Perception and Transduction Mechanisms of Cold Stress in Arabidopsis and Rice

Plants ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 1864
Author(s):  
Xiaoshuang Wei ◽  
Shuang Liu ◽  
Cheng Sun ◽  
Guosheng Xie ◽  
Lingqiang Wang
Keyword(s):  
Cold Stress ◽  
Plant Species ◽  
Freezing Tolerance ◽  
Chilling Stress ◽  
Deep Understanding ◽  
Freezing Stress ◽  
Future Perspective ◽  
Stress Signaling ◽  
Model Plant ◽  
Signal Perception

Cold stress, including freezing stress and chilling stress, is one of the major environmental factors that limit the growth and productivity of plants. As a temperate dicot model plant species, Arabidopsis develops a capability to freezing tolerance through cold acclimation. The past decades have witnessed a deep understanding of mechanisms underlying cold stress signal perception, transduction, and freezing tolerance in Arabidopsis. In contrast, a monocot cereal model plant species derived from tropical and subtropical origins, rice, is very sensitive to chilling stress and has evolved a different mechanism for chilling stress signaling and response. In this review, the authors summarized the recent progress in our understanding of cold stress response mechanisms, highlighted the convergent and divergent mechanisms between Arabidopsis and rice plasma membrane cold stress perceptions, calcium signaling, phospholipid signaling, MAPK cascade signaling, ROS signaling, and ICE-CBF regulatory network, as well as light-regulated signal transduction system. Genetic engineering approaches of developing freezing tolerant Arabidopsis and chilling tolerant rice were also reviewed. Finally, the future perspective of cold stress signaling and tolerance in rice was proposed.

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

2020 ◽  
Vol 477 (7) ◽  
pp. 1219-1225 ◽  
Author(s):  
Nikolai N. Sluchanko
Keyword(s):  
Protein Function ◽  
Intrinsically Disordered Protein ◽  
Structural Basis ◽  
Major Protein ◽  
Post Translational Modifications ◽  
Protein Protein Interaction ◽  
Intrinsically Disordered ◽  
Biochemical Journal ◽  
Multiple Binding ◽  
And Control

Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation. Phosphorylation can directly affect protein function and control recognition by proteins that ‘read’ the phosphorylation code, re-wiring the interactome. The eukaryotic 14-3-3 proteins recognizing multiple phosphoproteins nicely exemplify these concepts. Although recent studies established the biochemical and structural basis for the interaction of the 14-3-3 dimers with several phosphorylated clients, understanding their assembly with partners phosphorylated at multiple sites represents a challenge. Suboptimal sequence context around the phosphorylated residue may reduce binding affinity, resulting in quantitative differences for distinct phosphorylation sites, making hierarchy and priority in their binding rather uncertain. Recently, Stevers et al. [Biochemical Journal (2017) 474: 1273–1287] undertook a remarkable attempt to untangle the mechanism of 14-3-3 dimer binding to leucine-rich repeat kinase 2 (LRRK2) that contains multiple candidate 14-3-3-binding sites and is mutated in Parkinson's disease. By using the protein-peptide binding approach, the authors systematically analyzed affinities for a set of LRRK2 phosphopeptides, alone or in combination, to a 14-3-3 protein and determined crystal structures for 14-3-3 complexes with selected phosphopeptides. This study addresses a long-standing question in the 14-3-3 biology, unearthing a range of important details that are relevant for understanding binding mechanisms of other polyvalent proteins.

Sign in / Sign up

Export Citation Format

Share Document