Do chaperone proteins misfold?
Clash Royale CLAN TAG#URR8PPP
$begingroup$
If molecular chaperone proteins assist in the folding process of other proteins and misfolded proteins, can chaperone themselves misfold since they are also proteins? What would happen if chaperones misfolded? Can they misfold at all? Why or why not?
biochemistry molecular-biology proteins protein-folding
edited Feb 21 at 2:25
forest
236213
asked Feb 21 at 0:37
user3665690user3665690
534
$endgroup$
add a comment |
$begingroup$
If molecular chaperone proteins assist in the folding process of other proteins and misfolded proteins, can chaperone themselves misfold since they are also proteins? What would happen if chaperones misfolded? Can they misfold at all? Why or why not?
biochemistry molecular-biology proteins protein-folding
edited Feb 21 at 2:25
forest
236213
asked Feb 21 at 0:37
user3665690user3665690
534
$endgroup$
1
$begingroup$
Someone proposed this interesting hypothesis that misfolded chaperones can misfold other proteins and/or create more misfolded chaperones. Thus prions may be some kind of misfolded chaperones.
$endgroup$
– WYSIWYG
Feb 21 at 10:20
add a comment |
$begingroup$
If molecular chaperone proteins assist in the folding process of other proteins and misfolded proteins, can chaperone themselves misfold since they are also proteins? What would happen if chaperones misfolded? Can they misfold at all? Why or why not?
biochemistry molecular-biology proteins protein-folding
edited Feb 21 at 2:25
forest
236213
asked Feb 21 at 0:37
user3665690user3665690
534
$endgroup$
If molecular chaperone proteins assist in the folding process of other proteins and misfolded proteins, can chaperone themselves misfold since they are also proteins? What would happen if chaperones misfolded? Can they misfold at all? Why or why not?
biochemistry molecular-biology proteins protein-folding
biochemistry molecular-biology proteins protein-folding
edited Feb 21 at 2:25
forest
236213
asked Feb 21 at 0:37
user3665690user3665690
534
edited Feb 21 at 2:25
forest
236213
asked Feb 21 at 0:37
user3665690user3665690
534
edited Feb 21 at 2:25
forest
236213
edited Feb 21 at 2:25
forest
236213
edited Feb 21 at 2:25
forest
236213
236213
asked Feb 21 at 0:37
user3665690user3665690
534
asked Feb 21 at 0:37
user3665690user3665690
534
asked Feb 21 at 0:37
user3665690user3665690
534
534
1
$begingroup$
Someone proposed this interesting hypothesis that misfolded chaperones can misfold other proteins and/or create more misfolded chaperones. Thus prions may be some kind of misfolded chaperones.
$endgroup$
– WYSIWYG
Feb 21 at 10:20
add a comment |
1
$begingroup$
Someone proposed this interesting hypothesis that misfolded chaperones can misfold other proteins and/or create more misfolded chaperones. Thus prions may be some kind of misfolded chaperones.
$endgroup$
– WYSIWYG
Feb 21 at 10:20
1
1
$begingroup$
Someone proposed this interesting hypothesis that misfolded chaperones can misfold other proteins and/or create more misfolded chaperones. Thus prions may be some kind of misfolded chaperones.
$endgroup$
– WYSIWYG
Feb 21 at 10:20
$begingroup$
Someone proposed this interesting hypothesis that misfolded chaperones can misfold other proteins and/or create more misfolded chaperones. Thus prions may be some kind of misfolded chaperones.
$endgroup$
– WYSIWYG
Feb 21 at 10:20
add a comment |
1 Answer
1
active
oldest
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$begingroup$
Chaperone proteins are still proteins and they can certainly misfold just like any other. If that happens, it will either be assisted by another chaperone and given time to fold successfully or it will be destroyed. If this is happening too often and the amount of chaperones drops too low or the number of unfolded or incorrectly folded proteins becomes excessive*, the unfolded protein response may be triggered and, if it does not resolve the issue and the cell remains stressed, the cell will undergo apoptosis and die.
Some chaperones, especially heat-shock proteins, may be more resistant to misfolding. This is true because they need to be able to withstand noxious conditions that denature other proteins. Not all chaperones are resistant to heat though and many are no more intrinsically resistant to denaturing.
* It's not uncommon for a "bad" batch of proteins to be created. This can happen with a transcription error during mRNA synthesis since each mRNA molecule is read by many ribosomes. This can naturally happen with chaperones as well.
answered Feb 21 at 1:32
forestforest
236213
$endgroup$
$begingroup$
Good answer but it would be great if you can add some references for chaperones rescuing other misfolded chaperones. If you cannot find references (which, for this topic, I can understand) then you can indicate that this is your speculation.
$endgroup$
– WYSIWYG
Feb 21 at 9:47
$begingroup$
@WYSIWYG Many chaperones are non-specific in their interactions. For some reason I'm unable to access NIH right now (my IP is blocked), but a search shows examples of non-specific chaperone-mediated folding.
$endgroup$
– forest
Feb 21 at 10:40
$begingroup$
researchgate.net/post/…
$endgroup$
– forest
Feb 21 at 10:46
$begingroup$
I did a search on this topic myself but could not find any resourceful articles (researchgate is as good as stackexchange and even it doesn't have conclusive answers on this topic). So, I won't blame you.
$endgroup$
– WYSIWYG
Feb 21 at 11:05
add a comment |
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$begingroup$
Chaperone proteins are still proteins and they can certainly misfold just like any other. If that happens, it will either be assisted by another chaperone and given time to fold successfully or it will be destroyed. If this is happening too often and the amount of chaperones drops too low or the number of unfolded or incorrectly folded proteins becomes excessive*, the unfolded protein response may be triggered and, if it does not resolve the issue and the cell remains stressed, the cell will undergo apoptosis and die.
Some chaperones, especially heat-shock proteins, may be more resistant to misfolding. This is true because they need to be able to withstand noxious conditions that denature other proteins. Not all chaperones are resistant to heat though and many are no more intrinsically resistant to denaturing.
* It's not uncommon for a "bad" batch of proteins to be created. This can happen with a transcription error during mRNA synthesis since each mRNA molecule is read by many ribosomes. This can naturally happen with chaperones as well.
answered Feb 21 at 1:32
forestforest
236213
$endgroup$
$begingroup$
Good answer but it would be great if you can add some references for chaperones rescuing other misfolded chaperones. If you cannot find references (which, for this topic, I can understand) then you can indicate that this is your speculation.
$endgroup$
– WYSIWYG
Feb 21 at 9:47
$begingroup$
@WYSIWYG Many chaperones are non-specific in their interactions. For some reason I'm unable to access NIH right now (my IP is blocked), but a search shows examples of non-specific chaperone-mediated folding.
$endgroup$
– forest
Feb 21 at 10:40
$begingroup$
researchgate.net/post/…
$endgroup$
– forest
Feb 21 at 10:46
$begingroup$
I did a search on this topic myself but could not find any resourceful articles (researchgate is as good as stackexchange and even it doesn't have conclusive answers on this topic). So, I won't blame you.
$endgroup$
– WYSIWYG
Feb 21 at 11:05
add a comment |
$begingroup$
Chaperone proteins are still proteins and they can certainly misfold just like any other. If that happens, it will either be assisted by another chaperone and given time to fold successfully or it will be destroyed. If this is happening too often and the amount of chaperones drops too low or the number of unfolded or incorrectly folded proteins becomes excessive*, the unfolded protein response may be triggered and, if it does not resolve the issue and the cell remains stressed, the cell will undergo apoptosis and die.
Some chaperones, especially heat-shock proteins, may be more resistant to misfolding. This is true because they need to be able to withstand noxious conditions that denature other proteins. Not all chaperones are resistant to heat though and many are no more intrinsically resistant to denaturing.
* It's not uncommon for a "bad" batch of proteins to be created. This can happen with a transcription error during mRNA synthesis since each mRNA molecule is read by many ribosomes. This can naturally happen with chaperones as well.
answered Feb 21 at 1:32
forestforest
236213
$endgroup$
$begingroup$
Good answer but it would be great if you can add some references for chaperones rescuing other misfolded chaperones. If you cannot find references (which, for this topic, I can understand) then you can indicate that this is your speculation.
$endgroup$
– WYSIWYG
Feb 21 at 9:47
$begingroup$
@WYSIWYG Many chaperones are non-specific in their interactions. For some reason I'm unable to access NIH right now (my IP is blocked), but a search shows examples of non-specific chaperone-mediated folding.
$endgroup$
– forest
Feb 21 at 10:40
$begingroup$
researchgate.net/post/…
$endgroup$
– forest
Feb 21 at 10:46
$begingroup$
I did a search on this topic myself but could not find any resourceful articles (researchgate is as good as stackexchange and even it doesn't have conclusive answers on this topic). So, I won't blame you.
$endgroup$
– WYSIWYG
Feb 21 at 11:05
add a comment |
$begingroup$
Chaperone proteins are still proteins and they can certainly misfold just like any other. If that happens, it will either be assisted by another chaperone and given time to fold successfully or it will be destroyed. If this is happening too often and the amount of chaperones drops too low or the number of unfolded or incorrectly folded proteins becomes excessive*, the unfolded protein response may be triggered and, if it does not resolve the issue and the cell remains stressed, the cell will undergo apoptosis and die.
Some chaperones, especially heat-shock proteins, may be more resistant to misfolding. This is true because they need to be able to withstand noxious conditions that denature other proteins. Not all chaperones are resistant to heat though and many are no more intrinsically resistant to denaturing.
* It's not uncommon for a "bad" batch of proteins to be created. This can happen with a transcription error during mRNA synthesis since each mRNA molecule is read by many ribosomes. This can naturally happen with chaperones as well.
answered Feb 21 at 1:32
forestforest
236213
$endgroup$
Chaperone proteins are still proteins and they can certainly misfold just like any other. If that happens, it will either be assisted by another chaperone and given time to fold successfully or it will be destroyed. If this is happening too often and the amount of chaperones drops too low or the number of unfolded or incorrectly folded proteins becomes excessive*, the unfolded protein response may be triggered and, if it does not resolve the issue and the cell remains stressed, the cell will undergo apoptosis and die.
Some chaperones, especially heat-shock proteins, may be more resistant to misfolding. This is true because they need to be able to withstand noxious conditions that denature other proteins. Not all chaperones are resistant to heat though and many are no more intrinsically resistant to denaturing.
* It's not uncommon for a "bad" batch of proteins to be created. This can happen with a transcription error during mRNA synthesis since each mRNA molecule is read by many ribosomes. This can naturally happen with chaperones as well.
answered Feb 21 at 1:32
forestforest
236213
edited Feb 21 at 1:44
answered Feb 21 at 1:32
forestforest
236213
answered Feb 21 at 1:32
forestforest
236213
answered Feb 21 at 1:32
forestforest
236213
236213
$begingroup$
Good answer but it would be great if you can add some references for chaperones rescuing other misfolded chaperones. If you cannot find references (which, for this topic, I can understand) then you can indicate that this is your speculation.
$endgroup$
– WYSIWYG
Feb 21 at 9:47
$begingroup$
@WYSIWYG Many chaperones are non-specific in their interactions. For some reason I'm unable to access NIH right now (my IP is blocked), but a search shows examples of non-specific chaperone-mediated folding.
$endgroup$
– forest
Feb 21 at 10:40
$begingroup$
researchgate.net/post/…
$endgroup$
– forest
Feb 21 at 10:46
$begingroup$
I did a search on this topic myself but could not find any resourceful articles (researchgate is as good as stackexchange and even it doesn't have conclusive answers on this topic). So, I won't blame you.
$endgroup$
– WYSIWYG
Feb 21 at 11:05
add a comment |
$begingroup$
Good answer but it would be great if you can add some references for chaperones rescuing other misfolded chaperones. If you cannot find references (which, for this topic, I can understand) then you can indicate that this is your speculation.
$endgroup$
– WYSIWYG
Feb 21 at 9:47
$begingroup$
@WYSIWYG Many chaperones are non-specific in their interactions. For some reason I'm unable to access NIH right now (my IP is blocked), but a search shows examples of non-specific chaperone-mediated folding.
$endgroup$
– forest
Feb 21 at 10:40
$begingroup$
researchgate.net/post/…
$endgroup$
– forest
Feb 21 at 10:46
$begingroup$
I did a search on this topic myself but could not find any resourceful articles (researchgate is as good as stackexchange and even it doesn't have conclusive answers on this topic). So, I won't blame you.
$endgroup$
– WYSIWYG
Feb 21 at 11:05
$begingroup$
Good answer but it would be great if you can add some references for chaperones rescuing other misfolded chaperones. If you cannot find references (which, for this topic, I can understand) then you can indicate that this is your speculation.
$endgroup$
– WYSIWYG
Feb 21 at 9:47
$begingroup$
Good answer but it would be great if you can add some references for chaperones rescuing other misfolded chaperones. If you cannot find references (which, for this topic, I can understand) then you can indicate that this is your speculation.
$endgroup$
– WYSIWYG
Feb 21 at 9:47
$begingroup$
@WYSIWYG Many chaperones are non-specific in their interactions. For some reason I'm unable to access NIH right now (my IP is blocked), but a search shows examples of non-specific chaperone-mediated folding.
$endgroup$
– forest
Feb 21 at 10:40
$begingroup$
@WYSIWYG Many chaperones are non-specific in their interactions. For some reason I'm unable to access NIH right now (my IP is blocked), but a search shows examples of non-specific chaperone-mediated folding.
$endgroup$
– forest
Feb 21 at 10:40
$begingroup$
researchgate.net/post/…
$endgroup$
– forest
Feb 21 at 10:46
$begingroup$
researchgate.net/post/…
$endgroup$
– forest
Feb 21 at 10:46
$begingroup$
I did a search on this topic myself but could not find any resourceful articles (researchgate is as good as stackexchange and even it doesn't have conclusive answers on this topic). So, I won't blame you.
$endgroup$
– WYSIWYG
Feb 21 at 11:05
$begingroup$
I did a search on this topic myself but could not find any resourceful articles (researchgate is as good as stackexchange and even it doesn't have conclusive answers on this topic). So, I won't blame you.
$endgroup$
– WYSIWYG
Feb 21 at 11:05
add a comment |
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$begingroup$
Someone proposed this interesting hypothesis that misfolded chaperones can misfold other proteins and/or create more misfolded chaperones. Thus prions may be some kind of misfolded chaperones.
$endgroup$
– WYSIWYG
Feb 21 at 10:20