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Related Concept Videos

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
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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.
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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Post-translational Translocation of Proteins to the RER01:27

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Thermodynamic profiles for cotranslational trigger factor substrate recognition.

Therese W Herling1, Anaïs M E Cassaignau2, Anne S Wentink2

  • 1Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.

Science Advances
|July 10, 2024
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Summary
This summary is machine-generated.

Trigger factor (TF) molecular chaperone binds ribosomes with micromolar affinity, driven by enthalpy. It achieves nanomolar affinity for nascent chains via entropy, enabling broad substrate specificity.

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Area of Science:

  • Molecular biology
  • Biochemistry
  • Cellular proteostasis

Background:

  • Molecular chaperones maintain proteostasis, ensuring protein health.
  • Trigger factor (TF) is a crucial chaperone, acting early in protein synthesis.
  • TF's broad substrate specificity is not fully understood.

Purpose of the Study:

  • To elucidate the thermodynamic basis of Trigger factor's substrate interactions.
  • To understand how TF achieves favorable binding to diverse nascent proteins.

Main Methods:

  • Utilized microfluidics to investigate TF-ribosome interactions.
  • Analyzed thermodynamic contributions (enthalpy and entropy) to binding affinity.

Main Results:

  • TF binding to empty 70S ribosomes is enthalpy-driven (micromolar affinity).
  • TF achieves nanomolar affinity for nascent chains through favorable entropy.
  • Binding relies on TF-substrate groove occupation, not specific complementarity.

Conclusions:

  • TF employs a general mechanism for cotranslational function.
  • Favorable entropy drives high-affinity interactions with diverse nascent chains.
  • Insights into chaperone broad substrate specificity and proteostasis maintenance.