Unravelling chloroplast protein quality control in plants

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Pablo Pulido


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Chloroplasts are the organelles that define plants. In plants, they are the unique sites of photosynthesis, the only significant mechanism of energy input into the biosphere. They also mediate numerous essential biosynthetic processes and contribute to many other functions including stress responses. As a result, correct chloroplast performance is absolutely indispensable for plant fitness and agriculture. Plants are sessile organisms that display an astonishing capacity to adapt to adverse conditions including heat, cold, drought, and salinity. However, prolonged exposure to environmental stress inevitably results in productivity losses. These challenging conditions for plant growth are highly relevant in the context of climate change and food security.

One of the main problems that stresses cause at molecular level is protein misfolding and aggregation. Recycling of damaged proteins is achieved by the action of molecular chaperones but, when recycling is not possible, toxic aggregated proteins have to be degraded by the action of proteases to avoid cellular damage. Chaperones and proteases act coordinately and constitute protein quality control (PQC) systems that are required for organismal survival. In our project, we address the characterization of the chloroplast proteostasis network. It is long known for instance that the chaperone HSP70 posttranslationally regulates important chloroplast processes such as photosynthesis. However, the precise molecular mechanisms of the chaperone action remain unresolved. Importantly, the specificity of HSP70 is driven by its DNAJ partners, adaptors that recognise unfolded substrates and transfer them to the chaperone for refolding. Thus, DNAJs are useful tools for plant editing. Besides, disrupted proteostasis results in protein aggregation inside chloroplasts triggering a chloroplast-to-nucleus retrograde signal that regulates the expression of nuclear genes encoding plastid-targeted chaperones. Ultimately, an essential hallmark of the project is to gain knowledge for rational engineering of chloroplast proteostasis and nuclear reprogramming that will assist to manipulate crops stress resistance.

pulido fig1

Figure Legend: Figure. Canonical and non-canonical DNAJ proteins in plants. A, Traditional balanced model for proteostasis. Unfolded or aggregated substrates are refolded by molecular chaperones or degraded by the action of proteases. B, Proposed model of distinct mechanisms of protection from aggregation by canonical (HSP70-dependent: A to C types) and non-canonical (HSP70-independent: D to F types) DNAJ proteins. C, Schematic depiction of characteristic domains of DNAJ proteins in plants: J-domain (required for HSP70’s interaction), zinc finger domain (involved in protein-protein interactions), and C-terminal domain (also performs task of interaction with substrates) (Pulido and Leister, 2018).


 


Pulidolab2022 Laboratory Members

Name
Position
Contact
Pablo Pulido Talent Attraction Researcher
Jorge Vicente Postdoctoral Researcher

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