Role of Plant Endoplasmic Reticulum in Heat Stress

Among the different environmental inputs, heat stress (HS) is a major factor limiting crop productivity and plant geographic distribution. The HS has a negative effect on seed germination, photosynthetic capacity, cell growth and division, and crop yield and quality. Nonetheless, plants have evolved complex molecular networks that adjust their cellular metabolism to cope with heat stress. The deleterious effect of heat stress is the accumulation of unfolded proteins in the endoplasmic reticulum (ER). Thus, unfolded protein sensors in the ER are thought to play an essential role in heat tolerance.

Lifeasible is committed to analyzing the role of plant endoplasmic reticulum in heat stress for scientific and clinical purposes. ​Our experienced scientists and technicians can provide comprehensive customized services for analysis at all stages. With novel strategies and proprietary features of our platform, we can adjust to meet the needs of each client.

Unfolded Protein Sensors in Response to Heat Stress

• Under HS, the presence of misfolded proteins in the lumen of the ER is perceived as ER stress by the presence of specific proteins in the ER membrane, which activates the unfolded protein response (UPR). The UPR maintains ER homeostasis by inducing specific genes that code for chaperons and other proteins.

Fig.1. A generalized depiction of the temperature sensing mechanism in plants.

• Lifeasible provides analyses for the exploration basic leucine zipper (bZIP) transcription factor to reveal the response of the UPR to heat stress. The bZIP28 transcription factor is a type II membrane protein that has been identified as a stress sensor of the ER in plants. We provide structural analysis of the bZIP28 protein, analysis of the interaction with ER chaperones, and expression analysis of activated stress-responsive genes.
• In addition, we also provide an exploration of RNA splicing factors to uncover the response of the UPR to heat stress, including analysis of binding to unfolded proteins, excision base-pair fragments from mRNA, and others.

ER-Associated Degradation in Response to Heat Stress

• Endoplasmic reticulum associated degradation (ERAD) is a component of the ER quality control system, which removes misfolded proteins through the ubiquitin / proteasome-mediated degradation. The conserved genes DOA10 and HRD1 in the ERAD pathway play a regulatory role in heat stress response.
• We provide functional analyses of DOA10 and HRD1 in response to heat stress, as well as regulatory analyses of downstream gene transcription. It includes cultivation, identification, and phenotypic observation of plant mutants, quantitative RT-PCR, and others.

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