Heat Shock Proteins & Protein Folding: How HSP Helps

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SUMMARY

Heat Shock Proteins (HSPs) are crucial for protein folding, preventing misfolding and tangling in the cytoplasm. They function primarily as chaperones for newly synthesized proteins and assist in refolding stress-damaged proteins. HSPs are produced in greater quantities following stress events, and their activity is specific to certain protein species and conditions. During cellular stress, eukaryotic cells shift from cap-dependent to cap-independent translation, which selectively promotes the synthesis of stress-related proteins, including HSPs, thereby optimizing the folding process.

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  • Understanding of protein synthesis mechanisms in eukaryotic cells
  • Knowledge of Heat Shock Proteins and their functions
  • Familiarity with translation processes, specifically cap-dependent and cap-independent translation
  • Basic concepts of cellular stress responses
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  • Research the specific roles of different Heat Shock Proteins in cellular stress responses
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Cell biologists, molecular biologists, and researchers focused on protein folding and stress responses in eukaryotic organisms.

Priyadarshini
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I was watching a video in which they said that HSP is produced to help proteins fold correctly and to prevent them from tangling up and misfolding. But, if the cell is producing another protein, wouldn't the chances of tangling up and misfolding increase (because now you have one extra protein to the already crowded cell cytoplasm), even though this other protein (HSP) is produced to aid proteins fold correctly?
 
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HSP's do two "things":
1. chaperone newly synthesized proteins to allow correct folding
2. help stress damaged proteins return to the correct folded state.
so, we can say they are very targeted and work only with certain proteins in defined states of disarray.
They are increased in number post-stress events.

So particular HSP's are active only for certain protein species, and only under certain circumstances. They are not mass intruders into cytoplasm, attacking any and every wandering protein.
Try:
https://en.wikipedia.org/wiki/Heat_shock_protein
 
During stress, cells often dramatically change which mRNAs get translated. Most translation in eukaryotic cells occurs through cap-dependent mechanism that rely on recruiting the ribosome to mRNAs containing a specific modified nucleoside at the 5' end of the mRNA. Under conditions of stress, the cell will decrease cap-dependent translation and instead prefer to perform cap-independent translation, which recruits the ribosome to specific mRNAs through other means (not all of which are well understood). Not all mRNAs can be translated in a cap-independent way, and many of the mRNAs that undergo cap-independent translation are involved in stress responses (such as the heat shock proteins). Therefore, because conditions of stress decrease cap-dependent translation, fewer proteins overall get translated. This decrease in translation helps ensure that the newly synthesized proteins get folded correctly by the limited pool of existing chaperone proteins.

(I'm not sure if the same applies to bacteria as capping is specific to eukaryotes)
 
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