chaperones proteins
Protein chaperones direct the folding of polypeptides into functional proteins, facilitate developmental signalling and, as heat-shock proteins (HSPs), can be indispensable for survival in unpredictable environments. The main HSP chaperone families also buffer phenotypic variation.
Chaperones can do this either directly through masking the phenotypic effects of mutant polypeptides by allowing their correct folding, or indirectly through buffering the expression of morphogenic variation in threshold traits by regulating signal transduction. Environmentally sensitive chaperone functions in protein folding and signal transduction have different potential consequences for the evolution of populations and lineages under selection in changing environments.
Members
hsp-70
hsp-90
Features
suppression of aggregate formation
Kenny-Caffey syndrome can be caused by mutations in the gene encoding tubulin-specific chaperone E (TBCE) (MIM.604934)
BCS1L gene mutations in 2q33-37 (GRACILE syndrome) (#12215968#) (BCS1L, a mitochondrial inner-membrane protein, is a chaperone necessary for the assembly of mitochondrial respiratory chain complex III.)
In polyglutamine diseases
References
Rutherford SL. Between genotype and phenotype: protein chaperones and evolvability. Nat Rev Genet. 2003 Apr;4(4):263-74. PMID: #12671657#
Opal P, Zoghbi HY. The role of chaperones in polyglutamine disease. Trends Mol Med. 2002 May;8(5):232-6. PMID: #12067633#
Slavotinek AM, Biesecker LG. Unfolding the role of chaperones and chaperonins in human disease. Trends Genet. 2001 Sep;17(9):528-35. PMID: #11525836#
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