Translation Regulation and Protein Folding

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About this Research Topic

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Background

Translation, the process that promotes the synthesis of proteins from mRNA, constitutes a fundamental step in gene expression. This process is highly regulated in eukaryotes during specific stages of development and in response to environmental challenges. Translation regulation, which can be general or/and extremely specific, allows an organism to adjust its energy consumption to a particular situation and regulate the synthesis of the specific proteins involved. During translation, the nascent polypeptide might expose hydrophobic side chains that should be rapidly buried in the internal core to avoid unproductive interactions and to promote successful folding into native conformation. For this, the majority of multidomain proteins depend on chaperones and co-chaperones that help proteins achieve high activity yields. This folding assistance is especially relevant during specific developmental processes and stress conditions which challenge the folding capacity of the cell. This effect is observed in the ER, where the accumulation of unfolded proteins promotes the activation of the unfolded protein response (UPR). Additionally, protein folding forms part of the protein quality control (QC) system, which promotes the degradation of unfolded proteins to maintain protein homeostasis in the cell.

In the last few years, the development of techniques such as super-resolution ribosome profiling or TRAP (Translating Ribosomes Affinity Purification) has highlighted the main role of translation regulation in the control of gene expression during plant development and in response to environmental cues. Despite these impressive advances, the knowledge about the possible mechanisms that regulate translation in plants and the identification of the potential mRNAs targeted by translation regulation is scarce.

In addition, recent advances in the regulation of key proteins involved in ER stress alleviation and the onset of the UPR have uncovered the relevant role of protein folding in this compartment during plant developmental transitions and in response to environmental cues. In addition, the involvement of specific co-chaperones in the control of hormonal networks has revealed the importance of specific accessory proteins for the precise folding of relevant proteins involved in perception and signaling. However, this is only the tip of the iceberg, since a profound knowledge of the regulation of protein folding and roles of the main chaperones, the accessory proteins, and their possible targets is still lacking.

This Research Topic aims to highlight the following topics:

• Identification of new proteins/mechanisms involved in translation regulation.
• Characterization of new mRNAs regulated at the translational level
• Identification of novel chaperones and co-chaperones involved in plant physiological responses.
• Studies to uncover regulatory mechanisms that impinge the expression and activity of plant chaperones and co-chaperones.
• Identification of client proteins and the study of their relevance in plant development and plant responses to abiotic and biotic stresses.

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Keywords: Ribosome, Polysome, riboseq, Translational enhancer, Translation factor, Chaperone, Co-chaperone, Folding, Quality control, ER stress, Unfolded protein response, Heat-shock protein

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