Show/Hide Menu
Hide/Show Apps
anonymousUser
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Açık Bilim Politikası
Açık Bilim Politikası
Frequently Asked Questions
Frequently Asked Questions
Browse
Browse
By Issue Date
By Issue Date
Authors
Authors
Titles
Titles
Subjects
Subjects
Communities & Collections
Communities & Collections
Essential Structural and Functional Features of Small Heat Shock Proteins in Molecular Chaperoning Process
Date
2009-06-01
Author
Kocabıyık, Semra
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
3
views
0
downloads
Small heat shock proteins are ubiquitously found in all three domains of life, although they are the most poorly conserved family of molecular chaperones. Their involvement in anti-stress mechanisms of the cells have been clearly demonstrated by induction of their expression in response to various environmental and pathological stresses. Small heat shock proteins comprise the most effective chaperone family concerning their unusual capacity of substrate binding. It is well documented that small heat shock proteins associate with unfolding substrate proteins and form large oligomeric complexes to prevent their aggregation and accumulation, that otherwise would impair the normal cell functions. The substrates captured by small heat shock proteins are further refolded to their native state by ATP depended chaperones. During heat stress, the induced expression and activation of the small heat shock proteins, might reflect that this mechanism of protein quality control contributes to acquired thermotolerance in hyperthermophilic archaea, as well.
Subject Keywords
Small heat shock porteins
,
Chaperone activity
,
Heat-shock
,
Hyperthermophilic archaea
URI
https://hdl.handle.net/11511/38692
Journal
PROTEIN AND PEPTIDE LETTERS
DOI
https://doi.org/10.2174/092986609788490249
Collections
Department of Biology, Article