Fusion Proteins Cpn10-E^rns with Properties of Generating CSFV-Neutralized Antibodies

IntroductionClassical swine fever(CSF), included in the listA of the Office International des Epizooties(OIE), is ahighly contagious disease of domestic pigs and is con-sidered as the mostharmful disease occurring in pigs allover the world[1]. Outbreaks o…     

The interactome of CCT complex – A computational analysis

The eukaryotic chaperonin, CCT (Chaperonin Containing TCP1 or TriC-TCP-1 Ring Complex) has been subjected to physical and genetic analyses in S. cerevisiae which can be extrapolated to human CCT (hCCT), owing to its structural and functional similarities with yeast CCT (yCCT). Studies on hCCT and its interactome acquire an additional dimension, as it has been implicated in several disease conditions like neurodegeneration and cancer. We attempt to study its stress response role in general, which will be reflected in the aspects of human diseases and yeast physiology, through computational analysis of the interactome. Towards consolidating and analysing the interactome data, we prepared and compared the unique CCT-interacting protein lists for S. cerevisiae and H. sapiens, performed GO term classification and enrichment studies which provide information on the diversity in CCT interactome, in terms of protein classes in the data set. Enrichment with disease-associated proteins and pathways highlight the medical importance of CCT. Different analyses converge, suggesting the significance of WD-repeat proteins, protein kinases and cytoskeletal proteins in the interactome. The prevalence of proteasomal subunits and ribosomal proteins suggest a possible cross-talk between protein-synthesis, folding and degradation machinery. A network of chaperones and chaperonins that function in combination can also be envisaged from the CCT interactome-Hsp70 interactome analysis.     

Utilization of microgravity to improve the crystal quality of biologically important proteins: chaperonin-60, GrpE, B-subunit of V-type ATPase, and MIF

Protein crystallization experiments under microgravity were performed by using commercial vapor diffusion apparatus (CVDA) hardware on the STS-84 shuttle mission. Chaperonin-60, GrpE, the B subunit of V-type ATPase, and the selenomethionine substituted proteins of macrophage migration inhibitory factor (MIF) were selected as target proteins. The results indicate that microgravity positively affected their crystal growth, supporting the practical utilization of microgravity for the protein structure determination.     

The chaperonin of the archaeonSulfolobus solfataricus

The chaperonin of the hyperthermophilic archaeonSulfolobus solfataricus, briefly Ssocpn, was purified by a fast and high-yield procedure. Ssocpn, a 920 kDa-complex of two different subunits, displays a potassium-dependent ATPase activity with a temperature optimum at 80°C. The ability of Ssocpn to function in vitro was investigated using different protein substrates. Ssocpn promotes correct refolding of thermophilic and mesophilic enzymes from their chemically unfolded state; moreover, Ssocpn prevents the irreversible inactivation of native proteins by suppressing their precipitation upon heating. Both the activity in assisting refolding of unfolded proteins and that in preventing heat denaturation of native proteins require the hydrolysis of ATP. The chaperone-based strategies in different technological fields are discussed, and the advantages in using archaeal chaperonins are underlined.