Alpha-lactalbumin possesses a novel calcium binding loop

Calcium performs a unique role in biology, achieving biological effects through highly specific interactions with and modulation of target proteins. It has been proposed that calcium-modulated proteins possess a characteristic, evolutionarily related, binding fold, known as the EF-hand. The high-resolution X-ray structure of alpha-lactalbumin reveals a Ca2+ binding fold that resembles an EF-hand only superficially and presumably has no evolutionary relationship with it. However, there is clear homology with the corresponding loop in c-type lysozyme (the 'parent' molecule of alpha-lactalbumin). This study, at 1.7 A resolution, represents one of the most accurate analyses of a calcium binding protein yet reported.     

Partial purification of an endogenous elicitor from suspension-cultured cells of red bean,Vigna angularis

Brief irradiation with a germicidal UV lamp of cells of red bean,Vigna angularis, cultured in suspension in a quartz flask caused the release into the culture medium of an endogenous substance with elicitor activity, as well as the accumulation of isoflavone glucoside stress metabolites in the cells. The active compound was fractionated using phenylalanine ammonia lyase (PAL)-inducing activity in fresh cells as a marker. The elicitor active principle appears to be a low molecular weight (<2000 MW) water-soluble acidic oligosaccharide.     

Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli

The use of lacZ gene fusions, producing a hybrid protein containing an amino terminus specified by a target gene fused to the functional carboxy terminus of beta-galactosidase, has facilitated the study of protein targeting in various organisms. One of the best characterized fusions in Escherichia coli is phi(lamB-lacZ)42-1(Hyb), which produces a hybrid protein with the signal sequence and 181 N-terminal amino acids of the exported protein LamB, attached to LacZ. In common with other LacZ hybrids, the LamB-LacZ(42-1) protein is poorly exported from E. coli, conferring a Lac+ phenotype. beta-Galactosidase activity decreases markedly when cells producing the LamB-LacZ protein are grown at 42 degrees C or when a heat-shock response is induced at lower temperatures by overproducing heat-shock factor RpoH3, indicating the LacZ hybrids are being efficiently targeted to the cell envelope. We now report that the heat-shock proteins DnaK and GroEL can, in sufficient amounts, decrease beta-galactosidase activity and facilitate the export of lacZ-hybrid proteins.