Chaperonin GroEL, strictly describing GroEL-GroES complex is categorized as one sub-family (Group I chaperonin) under the molecular chaperones, which are the ubiquitous stress proteins of mitochondrial and chloroplastal evolutionary origin. Group I chaperonins are proteins that assist protein folding and assembly, and participate in the control of membrane translocation. Many molecular and cell...

Porphyromonas gingivalis is associated with human periodontal disease. We cloned and sequenced the gene for heat shock protein 60 (GroEL, HSP60) from P. gingivalis FDC381. The identified clone carried a 2.6 kb DNA fragment which contained two open reading frames (ORFs) encoding a 9.6- and a 58.4-kDa protein. The translated amino acid sequence of these ORFs showed a high degree of homology with ...

The folding of many proteins including luciferase in vivo requires the assistance of molecular chaperone proteins. To understand how a chaperone targets luciferase, we took three luciferases that give different bioluminescence with the same luciferin substrate and with differences in homology. The three luciferase genes, firefly luciferase (FF-Luc) (from Pyrocoelia miyako), and red (RE-Luc) and...

To survive in a competitive world, cells must optimise both the rate of production and the yield of correctly folded proteins. Partially folded polypeptide chains, either newly made by ribosomes or emerging from mature proteins unfolded by stress, run the risk of aggregating with one another to the detriment of the organism, the worst consequences being neurodegenerative diseases such as Alzhei...

Class B scavenger receptors (SR-B) are lipoprotein receptors that also mediate pathogen recognition, phagocytosis, and clearance as well as pathogen-induced signaling. In this study we report that three members of the SR-B family, namely, CLA-1, CLA-2, and CD36, mediate recognition of bacteria not only through interaction with cell wall LPS but also with cytosolic chaperonin 60. HeLa cells stab...

Bartonellae are bacterial pathogens for a wide variety of mammals. In humans, bartonellosis can result in angioproliferative lesions that are potentially life threatening to the patient, including bacillary angiomatosis, bacillary peliosis, and verruga peruana. The results of this study show that Bartonella bacilliformis, the agent of Oroya fever and verruga peruana, produces a proteinaceous mi...

The full-length sequences of the groESL genes (also known as cpn10/60) of Streptococcus anginosus, Streptococcus constellatus, Streptococcus gordonii, and Streptococcus sanguis and the near full-length sequence of the groESL genes of Streptococcus intermedius, Streptococcus bovis, Streptococcus mitis, Streptococcus mutans, Streptococcus oralis, and Streptococcus salivarius were determined. The ...

The Escherichia coli chaperone GroEL epitomizes the group of chaperone proteins termed as chaperonins. The wealth of structural and functional information available for GroEL, and its accessory protein, the co-chaperonin GroES, has been of much value in deciphering the role of chaperonins in facilitating the folding of substrate proteins in the cell. The chaperonin machinery has a complex archi...

Soluble complexes between the tetradecameric chaperonin GroEL and integral membrane proteins can be efficiently formed by detergent dialysis. For example, GroEL14 was found to bind a limit of two molecules of bacteriorhodopsin (BR). The GroEL-solubilized BR molecules were rapidly ejected from the chaperonin complexes on the addition of ATP or adenosine 5'-[beta,gamma-imido]triphosphate but not ...

Genome sequencing revealed that all six chlamydiae genomes contain three groEL-like genes (groEL1, groEL2, and groEL3). Phylogenetic analysis of groEL1, groEL2, and groEL3 indicates that these genes are likely to have been present in chlamydiae since the beginning of the lineage. Comparison of deduced amino acid sequences of the three groEL genes with those of other organisms showed high homolo...