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groEL chaperonin GroEL [ Escherichia coli str. K-12 substr. DH10B ]

Gene ID: 6061450, discontinued on 20-May-2015
  • This record was discontinued.
Gene symbol
groEL
Gene description
chaperonin GroEL
Locus tag
ECDH10B_4336
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. DH10B (strain: K-12, substrain: DH10B)
Lineage
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia
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Genomic Sequence:
NC_010473.1

Go to nucleotide: Graphics FASTA GenBank

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The conserved C-terminal tails of GroEL are thus important for protein folding from the beginning to the end of the chaperonin reaction cycle.
    Title: The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein.
  2. Folding catalysis by GroEL/ES is required by a set of proteins to reach native state at a biologically relevant timescale, avoiding aggregation or degradation.
    Title: GroEL/ES chaperonin modulates the mechanism and accelerates the rate of TIM-barrel domain folding.
  3. Study shows that the symmetric pattern of the GroEL subunits is broken as the GroEL cis-ring apical domains reorient to accommodate the simultaneous binding of GroES and an incompletely folded substrate protein.
    Title: Visualizing GroEL/ES in the act of encapsulating a folding protein.
  4. Comparison of the kinetics in the absence and presence of potassium ion (K+) clearly demonstrates that the first fluorescence-increasing phase corresponds to bimolecular MgATP2-(absent) binding to GroEL.
    Title: Dissecting a bimolecular process of MgATP²- binding to the chaperonin GroEL.
  5. The capacity to rescue proteins from folding traps may explain the uniquely essential role of chaperonin cages (formed by GroEL and GroES) within the cellular chaperone network.
    Title: Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
  6. denatured proteins facilitate the dissociation of ADP from the trans-ring of GroEL and the concomitant association of ATP and the second GroES
    Title: Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex.
  7. In the presence of alpha-crystallin or GroEL the kinetic of GAPDH aggregation is changed from the diffusion-limited cluster-cluster aggregation to the reaction-limited cluster-cluster aggregation.
    Title: Comparative analysis of the effects of alpha-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase.
  8. Suggest that highly expressed genes cannot routinely use GroEL for error control so that codon usage has evolved to provide complementary error limitation.
    Title: GroEL dependency affects codon usage--support for a critical role of misfolding in gene evolution.
  9. results confirmed the previously proposed placement of K(+) next to the nucleotide-binding site and also identified additional binding sites that may be important for GroEL function and cooperativity.
    Title: Use of thallium to identify monovalent cation binding sites in GroEL.
  10. Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic conformational changes of GroEL which lead to co-chaperonin GroES binding and the efficient encapsulation of substrate refolding proteins.
    Title: Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins.
Submit: New GeneRIF Correction See all GeneRIFs (15)
Names
chaperonin GroEL
YP_001732912.1
  • 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_010473.1 Reference assembly

    Range
    4469410..4471056
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. YP_001732912.1 chaperonin GroEL [Escherichia coli str. K-12 substr. DH10B]

    Status: REVIEWED

Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
B1XDP7.1