Open main menu
Home
Random
Recent changes
Special pages
Community portal
Preferences
About Wikipedia
Disclaimers
Incubator escapee wiki
Search
User menu
Talk
Dark mode
Contributions
Create account
Log in
Editing
GroEL
(section)
Warning:
You are not logged in. Your IP address will be publicly visible if you make any edits. If you
log in
or
create an account
, your edits will be attributed to your username, along with other benefits.
Anti-spam check. Do
not
fill this in!
=== Common === Heat shock proteins are amongst the most [[Protein family|evolutionarily conserved of proteins]].<ref name=five/> The significant function, structural, and sequential homology between HSP60 and its prokaryotic homolog, groEL, demonstrates this level of conservation. Moreover, HSP60βs amino acid sequence bears a similarity to its homolog in [[plants]], [[bacteria]], and [[humans]].<ref name=seven>{{cite journal |vauthors=Johnson RB, etal |title=Cloning and characterization of the yeast chaperonin HSP60 gene |journal=Genetics |volume=84 |issue=2 |pages=295β300 |year=2003 |doi=10.1016/0378-1119(89)90503-9 |pmid=2575559}}</ref> Heat shock proteins are primarily responsible for maintaining the integrity of cellular proteins particularly in response to environmental changes. Stresses such as temperature, concentration imbalance, pH change, and toxins can all induce heat shock proteins to maintain the conformation of the cellβs proteins. HSP60 aids in the folding and conformation maintenance of approximately 15-30% of all cellular proteins.<ref name=six/> In addition to HSP60βs typical role as a heat shock protein, studies have shown that HSP60 plays an important role in the [[transport]] and maintenance of mitochondrial proteins as well as the [[Transmission (genetics)|transmission]] and [[DNA replication|replication]] of mitochondrial [[DNA]].
Edit summary
(Briefly describe your changes)
By publishing changes, you agree to the
Terms of Use
, and you irrevocably agree to release your contribution under the
CC BY-SA 4.0 License
and the
GFDL
. You agree that a hyperlink or URL is sufficient attribution under the Creative Commons license.
Cancel
Editing help
(opens in new window)