F
IPR001844

Chaperonin Cpn60/GroEL

InterPro entry
Short nameCpn60/GroEL
Overlapping
homologous
superfamilies
 
family relationships

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
[1]
. These `helper' molecules are referred to as molecular chaperones, a subfamily of which are the chaperonins
[2]
. 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
[1]
), and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions
[2]
. This entry represents the 60kDa chaperonin (Cpn60), its bacterial homologue groEL and RuBisCO subunit-binding protein
[6]
), which are mainly present in bacteria and eukaryots.

The 60kDa form of chaperonin is the immunodominant antigen of patients with Legionnaire's disease
[3]
, 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
[4]
, 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 70kDa heat-shock proteins
[3]
. The crystal structure of Escherichia coli GroEL has been resolved to 2.8A
[5]
.

References

1.Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ. Nature 333, 330-4, (1988). View articlePMID: 2897629

2.cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock. Prasad TK, Stewart CR. Plant Mol. Biol. 18, 873-85, (1992). View articlePMID: 1349837

3.Sequence analysis of the Legionella micdadei groELS operon. Hindersson P, Hoiby N, Bangsborg J. FEMS Microbiol. Lett. 61, 31-8, (1991). View articlePMID: 1672279

4.Cloning and nucleotide sequence of the Brucella abortus groE operon. Gor D, Mayfield JE. Biochim. Biophys. Acta 1130, 120-2, (1992). View articlePMID: 1347461

5.The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB. Nature 371, 578-86, (1994). View articlePMID: 7935790

6.cpnDB: a chaperonin sequence database. Hill JE, Penny SL, Crowell KG, Goh SH, Hemmingsen SM. Genome Res 14, 1669-75, (2004). PMID: 15289485

GO terms

cellular component

  • None

Cross References

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