H
IPR037124

GroES chaperonin superfamily

InterPro entry
Short nameChaperonin_GroES_sf
Overlapping entries
 

Description

The chaperonins are 'helper' molecules required for correct folding and subsequent assembly of some proteins
[3]
. These are required for normal cell growth
[1]
, 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)
[2]
.

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.Type I chaperonins: not all are created equal. Levy-Rimler G, Bell RE, Ben-Tal N, Azem A. FEBS Lett. 529, 1-5, (2002). View articlePMID: 12354603

3.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

Further reading

4. Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis. Schmidt A, Schiesswohl M, Volker U, Hecker M, Schumann W. J. Bacteriol. 174, 3993-9, (1992). View articlePMID: 1350777

5. Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES. Martin J, Geromanos S, Tempst P, Hartl FU. Nature 366, 279-82, (1993). View articlePMID: 7901771

GO terms

molecular function

  • None

cellular component

  • None
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