InterPro : IPR001844

Name  Chaperonin Cpn60 Short Name  Chaprnin_Cpn60
Type  Family Description  The assembly of proteins has been thought to be the sole result of properties inherent in the primary sequence of polypeptides themselves. In some cases, however, structural information from other protein molecules is required for correct folding and subsequent assembly into oligomers []. These `helper' molecules are referred to as molecular chaperones, a subfamily of which are the chaperonins []. They are required for normal cell growth (as demonstrated by the fact that no temperature sensitive mutants for the chaperonin genes can be found in the temperature range 20 to 43 degrees centigrade []), and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions []. Type I chaperonins present in eubacteria, mitochondria and chloroplasts require the concerted action of 2 proteins, chaperonin 60 (cpn60) and chaperonin 10 (cpn10). Type II chaperonins, found in eukaryotic cytosol and in Archaebacteria, comprise only a cpn60 member.The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between 6 to 8 identical subunits, whereas the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits []. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides as isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner [, ]. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.The 60 kDa form of chaperonin is the immunodominant antigen of patients with Legionnaire's disease [], and is thought to play a role in the protection of the Legionella spp. bacteria from oxygen radicals within macrophages. This hypothesis is based on the finding that the cpn60 gene is upregulated in response to hydrogen peroxide, a source of oxygen radicals. Cpn60 has also been found to display strong antigenicity in many bacterial species [], and has the potential for inducing immune protection against unrelated bacterial infections. The RuBisCO subunit binding protein (which has been implicated in the assembly of RuBisCO) and cpn60 have been found to be evolutionary homologues, the RuBisCO subunit binding protein having the C-terminal Gly-Gly-Met repeat found in all bacterial cpn60 sequences. Although the precise function of this repeat is unknown, it is thought to be important as it is also found in 70 kDa heat-shock proteins []. The crystal structure of Escherichia coliGroEL has been resolved to 2.8A [].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR018370 Chaperonin Cpn60, conserved site Chaperonin_Cpn60_CS Conserved_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR002423 Chaperonin Cpn60/TCP-1 Cpn60/TCP-1 Family

6 Publications

First Author Title Year Journal Volume Pages
Gor D Cloning and nucleotide sequence of the Brucella abortus groE operon. 1992 Biochim Biophys Acta 1130 120-2
Hindersson P Sequence analysis of the Legionella micdadei groELS operon. 1991 FEMS Microbiol Lett 61 31-8
Schmidt A Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis. 1992 J Bacteriol 174 3993-9
Hemmingsen SM Homologous plant and bacterial proteins chaperone oligomeric protein assembly. 1988 Nature 333 330-4
Braig K The crystal structure of the bacterial chaperonin GroEL at 2.8 A. 1994 Nature 371 578-86
Prasad TK cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock. 1992 Plant Mol Biol 18 873-85



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)