Heat shock proteins: molecular chaperones of protein biogenesis.

Molecular cloning and expression of a Penicillium citrinum allergen with sequence homology and antigenic crossreactivity to a hsp 70 human heat shock protein

“…Although the mechanism of hsp 70 action is still poorly understood, the hsp 70s have been implicated in a variety of essential cellular processes. They assist in the proper folding of polypeptides, inhibit protein aggregation, target misfolded protein for degradation, facilitate polypeptide translocation, and participate in dissassembling oligomeric structures [16][17][18]. In addition to functioning as molecular chaperones.…”

“…The library contained 4.5 x lO*" independent clones with the size of the cDNA insert greater than 400 bp. The cDNA clones containing DNA sequences of allergens were screened by plaque immunoassay of the IPTG-induced library essentially as described previously 18,9]. IgE plaque immunoassay was conducted by using lOOOOpfu on 15cm petri dishes and serum from an asthmatic patient diluted 1/2 in E. coli lysate.…”

Molecular cloning, expression, and characterization of dnaK in Streptococcus pneumoniae

“…The hsp is known to be highly conserved at the amino acid level and to function as a chaperone. As part of the major heat shock proteins, DnaK promotes proper folding and translocation of proteins [1,2] and is a candidate for major antigens in several pathogens [3].…”

Fingerprinting analysis ofOenococcus oenistrains under stress conditions

“…Several mechanisms enable O. oeni to withstand stress conditions: the generation of a proton motrice force (Salema et al, 1996), activation of membrane-bound H 1 -ATPase (Carretè et al, 2002), modification of membrane fluidity , Silveira et al, 2003 and stress protein synthesis (Guzzo et al, 2000). Many of these proteins function as molecular chaperons or protease that could participate in the refolding or degradation processes of denatured proteins in the cell (Craig et al, 1993).…”