60 encoding gene has been previously used for the identification of various Gram positive bacteria and a chaperonin
sequence database containing a large collections of sequences including gene cpn60 of T.
Citarrella et al., "Elevated blood Hsp60, its structural similarities and cross-reactivity with thyroid molecules, and its presence on the plasma membrane of oncocytes point to the chaperonin
as an immunopathogenic factor in Hashimoto's thyroiditis," Cell Stress and Chaperones, vol.
Bahar, "Coupling between global dynamics and signal transduction pathways: a mechanism of allostery for chaperonin
GroEL," Molecular BioSystems, vol.
The same concept was further proven by using whole-cell MALDI-TOF MS spectra which identified three specific biomarkers, namely the histone-like protein HU form B, the 10 kDa chaperonin
Cpn10, and the 50S ribosomal protein L24 that were found to be relatively conserved amongst the Francisella genus but enabling the distinction of subspecies owing to slight differences in their sequences .
Based on molecular weight, the protein band with decreased intensity is most probably the heat shock protein-60 (HSP-60) or known as chaperonin
[sup],, PDCD5 can also interact with other molecules such as nuclear factor-?B p65 to regulate apoptosis via small heterodimer partner protein [sup] and another protein, cytosolic chaperonin
containing tailless complex polypeptide one, partly by inhibiting [sz]-tubulin folding.
The five genes include contactin 3 (CNTN3); Chaperonin
Containing TCP1, Subunit 5 (CCT5); valyl-tRNA synthetase 2, mitochondrial (VARS2) and inositol polyphosphate-5-phosphatase J (INPP5J), Protein Phosphatase 4, Regulatory Subunit 2 (PPP4R2).
Subunits of the chaperonin
CCT interact with F-actin and influence cell shape and cytoskeletal assembly.
They identified three genetic pathways that appear to be involved: the TCP-1 ring complex chaperonin
, which helps proteins fold; mitochondrial electron transport chain complexes (mETC); and a suite of genes responsible for the body's circadian rhythm.
Abstract | View Record in Scopus | Cited By in Scopus (1; sequencing of the DNA (8); it is also a tool for monitoring in vivo protein folding and chaperonin
HSP are highly conserved and ubiquitously expressed proteins and function as an intracellular chaperonin
for other proteins.
(a) Cytoskeleton and Chaperonin
, stress, Metabolic enzymes related proteins and folding proteins 17.1% 26.5% 24.8% Proteins associated Proteins involved in Proteins associated with detoxification cell cycle with translation and 6.8% regulation 6.8% transduction 5.1% Proteins associated Proteins associated Extracellular with membrane with biodegradative proteins 3.5% activity 5.1% metabolism 4.3% (b) Secreted 1.3% Endoplasmic Golgi 1.3% reticulum and secreted 1.3% Cytoplasmic vesicles Mitochondrial and Nuclear and 1.3% plasma membrane 4.0% cytoplasmatic 9.4% Endoplasmic Mitochondrial 16.3% Cytoplasmatic 50.2% reticulum lumen 14.9%