High impact information on Hsp60

• We present here the molecular analysis of the hsp60 gene promoter region and of two Drosophila hsp60 ethyl methane sulfonate embryonic lethal alleles that have an identical phenotype [1].
• The predicted Dm CCT gamma aa sequence shares a high degree of sequence identity with gamma-orthologues from human (70%), mouse (70%), protozoa (60%) and yeast (60%), and also contains domains found in other chaperonins including bacterial GroEL, mitochondrial Hsp60 and plant Rubisco large subunit-binding protein [2].
• The 60-kDa heat shock protein family (Hsp60) is found in prokaryotes, mitochondria, and chloroplasts [3].
• The Hsp60 proteins promote proper protein folding by preventing aggregation [3].
• In contrast to these findings, immunoelectron microscopy studies, using a cpn60 monoclonal antibody, revealed mitochondrial and extramitochondrial (plasma membrane, nucleus) immunoreactive material in rat liver cells [4].

Biological context of Hsp60

• In the present study, we characterized the Hsp60C gene (at 25F region), which shows high sequence homology with the other three Hsp60 genes of D. melanogaster [5].

Anatomical context of Hsp60

• Furthermore, none of the cpn60 antibodies used in this study recognized blotted proteins from rat red blood cells [4].
• Several reports have claimed that the mitochondrial chaperonin cpn60, or a close homolog, is also present in some other subcellular compartments of the eukaryotic cell [4].

Analytical, diagnostic and therapeutic context of Hsp60

• Immunoelectron microscopy studies, using a polyclonal serum against cpn60, revealed that the protein is exclusively localized within the mitochondria of rat liver and embryonic Drosophila cells (SL2) [4].
• The monoclonal antibody, as well as cpn60 polyclonal sera, only recognize mitochondrial cpn60 in Western blots of liver proteins [4].

References