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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

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 Folding03:00

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...
Bacterial Protein Maturation01:26

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...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Structure and function of the molecular chaperone Trigger Factor.

Anja Hoffmann1, Bernd Bukau, Günter Kramer

  • 1Zentrum für Molekulare Biologie der Universität Heidelberg, Heidelberg, Germany.

Biochimica Et Biophysica Acta
|February 6, 2010
PubMed
Summary
This summary is machine-generated.

Newly synthesized proteins rely on molecular chaperones like Escherichia coli Trigger Factor for proper folding. This review details Trigger Factor

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Area of Science:

  • Molecular biology
  • Protein folding
  • Biochemistry

Background:

  • Newly synthesized proteins require molecular chaperones for correct folding.
  • Ribosome-associated chaperones initiate folding, while others assist post-translational folding.
  • Escherichia coli Trigger Factor is a key ribosome-associated chaperone.

Purpose of the Study:

  • To review current knowledge on Escherichia coli Trigger Factor.
  • To highlight recent advances in understanding Trigger Factor's structure, dynamics, and function.
  • To discuss Trigger Factor's roles in co-translational folding, ribosome-independent functions, and cooperation with other chaperones.

Main Methods:

  • Literature review of structural and dynamic studies.
  • Analysis of experimental data on Trigger Factor interactions.
  • Discussion of proposed functional mechanisms.

Main Results:

  • Trigger Factor interacts with the ribosome and substrates, influencing co-translational folding.
  • Trigger Factor has a newly proposed ribosome-independent function in protein complex assembly.
  • Functional cooperation exists between Trigger Factor, DnaK, and GroEL for cytosolic protein folding.

Conclusions:

  • Trigger Factor plays a crucial role in nascent polypeptide chain folding and processing.
  • Understanding Trigger Factor's multifaceted roles is essential for comprehending cellular protein homeostasis.
  • Further research into Trigger Factor's interactions and functions will advance the field of molecular chaperones.