Disease relevance of groS

• The temperature-sensitive mutants did not allow the propagation of phage lambda at 28 degrees C and formed long filamentous structures without septa at 41 degrees C, as is observed in the case of groES mutants [1].
• In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded polypeptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitochondria (hsp60) or chloroplasts (Rubisco sub-unit-binding protein), together with chaperonin-10 from E. coli (groES), and Mg-ATP [2].
• Sequence and transcriptional analysis of groES and groEL genes from the thermophilic bacterium Clostridium thermocellum [3].
• The cloning and sequencing of the Brucella abortus groES and groEL genes are reported [4].
• Cloning, characterization and functional analysis of groEL-like gene from thermophilic cyanobacterium Synechococcus vulcanus, which does not form an operon with groES [5].

High impact information on groS

• Thus during heat shock some groEL is reversibly phosphorylated, which allows its ATP-dependent release from protein substrates in the absence of its usual cofactor (groES), and probably promotes the repair of damaged polypeptides [6].
• Interaction requires Mg ions, whereas MgATP inhibits, and inhibition is stronger in the presence of co-chaperonin GroES. "Heat-shock" of the membrane at 45 degrees C destroys irreversibly its ability to bind GroEL [7].
• Identification of a groES-like chaperonin in mitochondria that facilitates protein folding [8].
• A second class of 8.3-kilobase inserts was shown to contain the groE region by (i) restriction analysis, (ii) Southern hybridization of the 8.3-kilobase insert to groE+ DNA, and (iii) identification of the gene products by similar migration on polyacrylamide gels [9].
• Furthermore, the extent to which assembly occurs is limited by the normal levels of expression of the groE operon (Goloubinoff, P., Gatenby, A. A., and Lorimer, G. H. (1989) Nature 337, 44-47) [10].

Chemical compound and disease context of groS

• The longest open reading frame potentially encodes a peptide of 431 amino acids and exhibits similarity to other eukaryotic ODCs, prokaryotic and eukaryotic arginine decarboxylases (ADCs), prokaryotic meso-diaminopimelate decarboxylases and the product of the tabA gene of Pseudomonas syringae cv. tabaci [11].

Biological context of groS

• These observations suggest to us that the morphogenesis gene groES plays a key role in coupling between replication of the F plasmid and cell division of the host cells [1].
• These results help explain why mutations in either of the groE genes exhibit similar phenotypes with respect to both lambda and bacterial growth [12].
• Subcloning demonstrated that an intact mutant groEL gene was necessary for suppression and that plasmids carrying the 8.3-kilobase insert could suppress mutants carrying groES- but not groEL- genes for phage lambda growth [9].
• A controlling inverted repeat of chaperone expression (CIRCE) element lies between the consensus promoter of the operon and TRt groES [13].
• Sequencing of 2,309 bp led to the detection of two open reading frames in the order groES groEL [14].

Associations of groS with chemical compounds

• We have studied how nucleotides (ADP, AMP-PNP, and ATP) and the co-chaperonin GroES influence the GroEL-affected refolding of apo-alpha-lactalbumin [15].

Analytical, diagnostic and therapeutic context of groS

• At various times during the groE-dependent renaturations, groEL was rapidly removed from the renaturation mixture by immunoprecipitation and centrifugation (30 s) [16].
• Sequence analysis and heterologous expression of the groE genes from Thermoanaerobacter sp. Rt8.G4 [13].
• The fragment was sequenced and the partial GroEL sequence was expanded by vectorette PCR upstream and downstream to cover the complete P. aeruginosa groE operon [17].
• The structural stability of the co-chaperonin GroES has been studied by high sensitivity differential scanning calorimetry and circular dichroism under different solvent conditions [18].

References