#hsp90 — Public Fediverse posts

These ‘master’ proteins protect us from deadly mutations — and could inspire new drugs.
Our genome is full of potentially dangerous mutations, which in most cases show no signs of harm. This paradox is explained by the existence of special "buffer" proteins that mask the harmful effects of genetic changes. A key role among these is played by the well-known heat shock protein HSP90, which acts as a molecular chaperone, helping other proteins fold into the correct three-dimensional structure even in the presence of mutations that could otherwise disrupt this process. Essentially, HSP90 serves as a kind of "fuse," allowing the body to accumulate latent genetic potential that can be activated when needed. Disabling the HSP90 gene in flies leads to massive developmental abnormalities, as if releasing the entire accumulated burden of latent mutations.
Modern research has identified a number of other buffer genes, including proteins involved in chromatin organization. During heat stress, such as during a fever, HSP90 reserves can be depleted, and then hidden problems begin to manifest.
Thus, the evolutionary and medical significance of buffer proteins extends far beyond basic biology. On the one hand, they form a "silent" genetic reserve that can suddenly be released when environmental conditions change (for example, during global warming), generating new adaptive traits and accelerating evolution. On the other hand, understanding these mechanisms opens up therapeutic possibilities.
However, I can't even begin to imagine how a single protein could correct the infinite variety of mutations in an infinite variety of protein topologies. I assume it only works with proteins of a certain topology and corrects only specific mutations, for example, at the site of an alpha helix fold—correcting it will restore the correct folding—or simply tightening up anything that's slipping, judging by its shape, or something similar.

https://www.nature.com/articles/d41586-026-01883-0

#science #science_news #chaperones #heat_shock_proteins #mutations #biology #HSP90

These ‘master’ proteins protect us from deadly mutations — and could inspire new drugs.
Our genome is full of potentially dangerous mutations, which in most cases show no signs of harm. This paradox is explained by the existence of special "buffer" proteins that mask the harmful effects of genetic changes. A key role among these is played by the well-known heat shock protein HSP90, which acts as a molecular chaperone, helping other proteins fold into the correct three-dimensional structure even in the presence of mutations that could otherwise disrupt this process. Essentially, HSP90 serves as a kind of "fuse," allowing the body to accumulate latent genetic potential that can be activated when needed. Disabling the HSP90 gene in flies leads to massive developmental abnormalities, as if releasing the entire accumulated burden of latent mutations.
Modern research has identified a number of other buffer genes, including proteins involved in chromatin organization. During heat stress, such as during a fever, HSP90 reserves can be depleted, and then hidden problems begin to manifest.
Thus, the evolutionary and medical significance of buffer proteins extends far beyond basic biology. On the one hand, they form a "silent" genetic reserve that can suddenly be released when environmental conditions change (for example, during global warming), generating new adaptive traits and accelerating evolution. On the other hand, understanding these mechanisms opens up therapeutic possibilities.
However, I can't even begin to imagine how a single protein could correct the infinite variety of mutations in an infinite variety of protein topologies. I assume it only works with proteins of a certain topology and corrects only specific mutations, for example, at the site of an alpha helix fold—correcting it will restore the correct folding—or simply tightening up anything that's slipping, judging by its shape, or something similar.

https://www.nature.com/articles/d41586-026-01883-0

#science #science_news #chaperones #heat_shock_proteins #mutations #biology #HSP90

New study discovers how altered #protein_folding drives #multicellular #evolution.

#yeast #Hsp90

https://phys.org/news/2024-03-protein-multicellular-evolution.html

Like comparing apples to apples, comparing similar #proteins can be challenging. #Scientists at #StJude developed a tool to help, which garnered new insights into the #ChaperoneProtein #HSP90—an essential target in #cancer. Read about their work. https://bit.ly/3LMhQVf #StJudeResearch #StructuralBiology #ChemicalBiology #DrugDiscovery