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Chloroplast precursor protein preClpD overaccumulation triggers multilevel reprogramming of gene expression and a heat shock-like response by Zheng-Hui Hong & Liyu Zhu & Lin-Lin Gao & Zhe Zhu & Tong Su & Leonard Krall & Xu-Na Wu & Ralph Bock & Guo-Zhang Wu ISBN 101038/S41467025590433 instant download

  • SKU: EBN-235045596
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Instant download (eBook) Chloroplast precursor protein preClpD overaccumulation triggers multilevel reprogramming of gene expression and a heat shock-like response after payment.
Authors:Zheng-Hui Hong & Liyu Zhu & Lin-Lin Gao & Zhe Zhu & Tong Su & Leonard Krall & Xu-Na Wu & Ralph Bock & Guo-Zhang Wu
Pages:updating ...
Year:2025
Publisher:x
Language:english
File Size:6.93 MB
Format:pdf
ISBNS:101038/S41467025590433
Categories: Ebooks

Product desciption

Chloroplast precursor protein preClpD overaccumulation triggers multilevel reprogramming of gene expression and a heat shock-like response by Zheng-Hui Hong & Liyu Zhu & Lin-Lin Gao & Zhe Zhu & Tong Su & Leonard Krall & Xu-Na Wu & Ralph Bock & Guo-Zhang Wu ISBN 101038/S41467025590433 instant download

Nature Communications, doi:10.1038/s41467-025-59043-3

Thousands of nucleus-encoded chloroplast proteins are synthesized as precursors on cytosolic ribosomes and posttranslationally imported into chloroplasts. Cytosolic accumulation of unfolded chloroplast precursor proteins(e.g., under stress conditions) is hazardous to the cell. The global cellularresponses and regulatory pathways involved in triggering appropriateresponses are largely unknown. Here, by inducible and constitutive overexpression of ClpD-GFP to result in precursor protein overaccumulation, wepresent a comprehensive picture of multilevel reprogramming of geneexpression in response to chloroplast precursor overaccumulation stress(cPOS), reveal a critical role of translational activation in the expression ofcytosolic chaperones (heat-shock proteins, HSPs), and demonstrate thatchloroplast-derived reactive oxygen species act as retrograde signal for thetranscriptional activation of small HSPs. Furthermore, we reveal an importantrole of the chaperone ClpB1/HOT1 in maintaining cellular proteostasis uponcPOS. Together, our observations uncover a cytosolic heat shock-like responseto cPOS and provide insights into the underlying molecular mechanisms.

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