Distinct character in hydrophobicity of amino acid compositions of mitochondrial proteins.
A compact mitochondrial gene contains all essential information about the synthesis of mitochondrial proteins which play their roles in a small compartment of the mitochondrium. Almost no noncoding regions have been found through the gene, but a necessary set of tRNAs for the 20 amino acids is provided for biosynthesis, some of them coding different amino acids from those in a usual cell. Since the gene is so compact that the produced proteins would have some characteristic aspects for the mitochondrium, amino acid compositions of mitochondrial proteins (mt-proteins) were examined in the 20-dimensional composition space. The results show that compositions of proteins translated from the mitochondrial genes have a distinct character having more hydrophobic content than others, which is illustrated by a clustered distribution in the multidimensional composition space. The cluster is located at the tail edge of the global distribution pattern of a Gaussian shape for other various kinds of proteins in the space. The mt-proteins are rich in hydrophobic amino acids as is a membrane protein, but are different from other membrane proteins in a lesser content of Val. A good correlation found between the base and amino acid compositions for the mitochondria was examined in comparison to those of organisms such as thermophilic bacterium having an extreme G-C-rich base composition.
Nakashima
H
H
Kanazawa University Kodatsuno 5-chome, Japan.
Nishikawa
K
K
Ooi
T
T
D000596:Amino Acids / Q000235:genetics*; D000818:Animals; D001482:Base Composition; D002417:Cattle; D004247:DNA / Q000737:chemistry; D016208:Databases, Factual; D006801:Humans; D051379:Mice; D008928:Mitochondria / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012995:Solubility
D000596:Amino Acids; D011506:Proteins; D004247:DNA