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Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

Protein Transport to the Stroma

Protein Transport to the Stroma

Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...

Protein Transport to the Inner Chloroplast Membrane

Protein Transport to the Inner Chloroplast Membrane

Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...

Protein Transport to the Outer Chloroplast Membrane

Protein Transport to the Outer Chloroplast Membrane

Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.

Bacterial Protein Maturation

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Updated: Apr 18, 2026

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

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ATP-dependent molecular chaperones in plastids--More complex than expected.

Raphael Trösch¹, Timo Mühlhaus², Michael Schroda²

¹TU Kaiserslautern, Molecular Biotechnology & Systems Biology, Paul-Ehrlich-Straße 23, 67663 Kaiserslautern, Germany; HU Berlin, Institute of Biology, Chausseestraße 117, 10115 Berlin, Germany; TU Kaiserslautern, Molecular Genetics of Eukaryotes, Paul-Ehrlich-Straße 23, 67663 Kaiserslautern, Germany.

Biochimica Et Biophysica Acta

|January 18, 2015

Summary

Molecular chaperones are vital for plant plastid function, assisting protein import, folding, and quality control. This review explores their general and specific roles, highlighting areas for future research in these essential organelles.

Keywords:

Abiotic stress Molecular chaperone Photosynthesis Plastid development Protein folding Protein homeostasis

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Last Updated: Apr 18, 2026

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

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Published on: September 28, 2018

Analysis of Protein Import into Chloroplasts Isolated from Stressed Plants

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Published on: November 1, 2016

Studying Protein Import into Chloroplasts Using Protoplasts

Studying Protein Import into Chloroplasts Using Protoplasts

Published on: December 10, 2018

Area of Science:

Plant Cell Biology
Molecular Biology
Organelle Biology

Background:

Plastids (chloroplasts, amyloplasts, chromoplasts) are crucial plant organelles.
They import most proteins, requiring molecular chaperones for processing.
Four major ATP-dependent chaperone families are found in plastids.

Purpose of the Study:

To review current knowledge on general and specific functions of plastid molecular chaperones.
To discuss the unique challenges and specialized roles of chaperones in plastids, especially chloroplasts.
To identify unsolved questions and guide future research directions.

Main Methods:

Literature review of existing research on plastid molecular chaperones.
Analysis of the roles of chaperones in protein import, folding, and quality control within plastids.
Discussion of the impact of the chloroplast environment on chaperone function.

Main Results:

Plastid chaperones (Cpn60, Hsp70, Hsp90, Hsp100) are essential for various protein management processes.
These chaperones perform both conserved and specific functions tailored to plastid environments.
The extreme conditions within chloroplasts suggest specialized chaperone adaptations.

Conclusions:

Plastid chaperones play indispensable roles in organelle biogenesis and function.
Further research is needed to fully understand the specific adaptations and functions of these chaperones.
Investigating plastid chaperones offers insights into plant cell resilience and adaptation.