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Biomedical subjects

J Someya

Publications and source records attributed to J Someya.

6 recordsLinked to original sources
PubMed1994

The gene for ribosomal protein L27 is located on the plastid rather than the nuclear genome of the chlorophyll c-containing alga Pleurochrysis carterae.

The gene for ribosomal protein L27 (rpl27) has not been found in plastid genomes. We report here that the rpl27 gene is located in the plastid genome of the prymnesiophyte Pleurochrysis carterae. The deduced amino acid sequence showed 59% identity with E. coli L27. 1.0 kb transcript of the gene was detected by Northern blot analysis. Nucleotide sequence analysis of PCR products suggested that rpl27 is widespread in the genomes of Prymesiophyta and Rhodophyta. In all species of Prymnesiophyta examined in this study, the gene is located at the 3' downstream region of Rubisco operon.

Amino Acid Sequence↗
PubMed1993

A molecular dynamics study of solvent behavior around a protein.

The solvent structure and behavior around a protein were examined by analyzing a trajectory of molecular dynamics simulation of the trp-holorepressor in a periodic box of water. The calculated self diffusion coefficient indicated that the solvent within 10 A of the protein had lower mobility. Examination of the solvent diffusion around different atoms of different kinds of residues showed no general tendency. This fact suggested that the solvent mobility is not influenced significantly by the kind of the atom or residue they solvated. Distribution analysis around the protein revealed two peaks of water oxygen: a sharp one at 2.8 A around polar and charged atoms and a broad one at approximately 3.4 A around apolar atoms. The former was stabilized by water-protein hydrogen bonds, and the latter was stabilized by water-water hydrogen bonds, suggesting the existence of a hydrophobic shell. An analysis of protein atom-water radial distribution functions confirmed these shell structures around polar or charged atoms and apolar ones.

Amino Acids↗
PubMed1992

Free energy perturbation study on a Trp-binding mutant (Ser88-->Cys) of the trp-repressor.

The Ser88-->Cys mutant of the trp-repressor showed a lower affinity for the corepressor than the wild-type repressor [delta delta G = 1.7 +/- 0.3 kcal/mol, Chou and Matthews (1989) J. Biol. Chem., 264, 18314-18319]. A molecular dynamics/free energy cycle perturbation study was performed to understand the origin of the decreased affinity. A value (delta delta G = 1.58 +/- 0.28 kcal/mol) comparable with the experimental value was obtained by the simulation. Free energy component analysis revealed that destabilization of the van der Waals interaction between Ser88 and Trp109 (corepressor) mainly contributed to the decreased affinity of the mutant. The rotational transition of the hydroxyl (sulfhydryl) group of Ser88 (Cys88) during the simulations affected the contributions of Arg84 and water to the free energy change in the aporepressor and those of Arg84 and Trp109 to that in the holorepressor. However, the contributions from different residues compensated each other, and the total free energy changes were almost invariable in the various simulations.

Bacterial Proteins↗
PubMed1991

Molecular dynamics simulation of trp-aporepressor in a solvent.

Molecular dynamics simulations of Escherichia coli trp-aporepressor were carried out in the absence and presence of explicit water molecules. The vacuum simulations resulted in significant deformation of the initial X-ray structure. A solvated simulation with a nonbonded cut-off radius of 9 A gave a better result, and the most satisfactory result was obtained when electrostatic interactions within a cut-off radius of 18 A were considered by a twin-range method. The trajectory from the last simulation was used to analyze the dynamical properties of the aporepressor. The root-mean-square fluctuations of the residues showed the rigidity of the central core and the flexibility of the DNA-binding sites, consistent with the X-ray temperature factors. The dynamical cross-correlation map indicated a significant negative correlation between the central core and the two DNA-binding sites, and thus reproduced the three-domain format (a central core and two DNA-binding heads) from a dynamical point of view. The core region showed weak, but many, intra- and inter-molecular correlations, while the helix-turn-helix DNA-binding motifs were free from correlations with other regions.

Apoproteins↗
PubMed1990

Oxygen resistant strain of N2-fixing Escherichia coli.

Oxygen resistant N2-fixing Escherichia coli, which can grow at a high oxygen concentration in a nitrogen-free medium, were produced by several times of cultivation under a condition of 0.03% oxygen. Six isolated resistant strains could grow at an oxygen concentration ten times that of the parent strain. The nif-genes of these six strains were integrated into a chromosome. At low oxygen, they showed one third the nitrogenase activity to the parent strain, but more so at a high oxygen concentration. It is thus evident that the amount of nitrogenase protein in a cell is a factor determining the oxygen resistance of nitrogenase.

Chromosomes, Bacterial↗