chaperonin


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Related to chaperonin: GroEL

chap·er·o·nin

 (shăp′ə-rō′nĭn)
n.
Any of a family of large chaperone proteins that function chiefly to assist in the folding of newly synthesized proteins.

References in periodicals archive ?
5S RNA signal recognition particle (RWLH04543), signal recognition particle subunit SRP54 (RWLH01652), protein translocase subunit SecB (RWLH02874), chaperone protein DnaJ (RWLH04040), chaperone protein DnaK (RWLH00991, RWLH04038, RWLH04039), GrpE protein (RWLH01655), chaperonin GroES (RWLH03651) and chaperonin GroEL (RWLH03652).
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 [23].
72] stated that glutathione, lipid hydroperoxides, and heat shock protein chaperonin 60 in the newborn's serum might have functional and diagnostic significance for oxidative stress.
Based on molecular weight, the protein band with decreased intensity is most probably the heat shock protein-60 (HSP-60) or known as chaperonin 60.
B p65 to regulate apoptosis via small heterodimer partner protein [sup][13] 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 activity [9].
The dark-expressed proteins not involved in photosynthesis and the Calvin cycle included a chloroplast 20 kDa chaperonin (spot9), S-adenosylmethionine synthase (spot 4), and a multi-peptide mixture containing three tubulin A proteins (spot 1).
Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
Many such mutualists constitutively over-express the chaperonin GroEL (Ishikawa, 1984), perhaps as a compensatory mechanism to cope with degraded protein structures (Moran, 1996).