A genetic code alteration generates a proteome of high diversity in the human pathogen <Emphasis Type="Italic">Candida albicans</Emphasis>

Background  

Genetic code alterations have been reported in mitochondrial, prokaryotic, and eukaryotic cytoplasmic translation systems, but their evolution and how organisms cope and survive such dramatic genetic events are not understood.     

The sorption of a protein-polysaccharide complex isolated from Neisseria meningitidis serogroup B on aluminum hydroxide gels and the immunological activity of the sorbed preparations

The protein-polysaccharide complex, isolated from group B N. meningitidis, is a variant of vaccine for the prophylaxis of group B N. meningitidis infection. In this investigation the influence of the complex of the physical properties of aluminium hydroxide gels, the amount of gel, pH and the duration of sorption on the process of sorption has been studied. Aluminium hydroxide has been shown to produce a stimulating effect on the response of mice to the polysaccharide and protein contained in the complex after immunization made in two injections. Gels with a smaller particle size have been found to possess greater adjuvant activity, as well as greater absorbing activity. The immunological activity of the complex, adsorbed ex tempore, has proved to be no different from that of the complex adsorbed in an hour.     

Structure of Flagellar Motor Proteins in Complex Allows for Insights into Motor Structure and Switching

The flagellar motor is one type of propulsion device of motile bacteria. The cytoplasmic ring (C-ring) of the motor interacts with the stator to generate torque in clockwise and counterclockwise directions. The C-ring is composed of three proteins, FliM, FliN, and FliG. Together they form the “switch complex” and regulate switching and torque generation. Here we report the crystal structure of the middle domain of FliM in complex with the middle and C-terminal domains of FliG that shows the interaction surface and orientations of the proteins. In the complex, FliG assumes a compact conformation in which the middle and C-terminal domains (FliG_MC) collapse and stack together similarly to the recently published structure of a mutant of FliG_MC with a clockwise rotational bias. This intramolecular stacking of the domains is distinct from the intermolecular stacking seen in other structures of FliG. We fit the complex structure into the three-dimensional reconstructions of the motor and propose that the cytoplasmic ring is assembled from 34 FliG and FliM molecules in a 1:1 fashion.