Distinct character in hydrophobicity of amino acid compositions of mitochondrial proteins
โ Scribed by Hiroshi Nakashima; Ken Nishikawa; Tatsuo Ooi
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 574 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
โฆ Synopsis
Abstract
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 mitrochondrium, amino acid compositions of mitochondrial proteins (mtโproteins) were examined in the 20โdimensional 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 mtโproteins 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 GโCโrich base composition.
๐ SIMILAR VOLUMES
The amino-acid compositions of the mitochondrial ribosomal subunits of Saccharomyces cerevisiae have been determined and compared to those of cytoplasmic ribosomal subunits. For the large subunits, the mitochondrial and cytoplasmic ribosomes showed major differences in the proportions of arginine, a
A critical overview is given on the application of amino acid composition data for the establishment of the protein's identity (amino acids composition vs. protein identity, the AAC-PI method). Several criteria are used to measure the differences between the amino acid compositions of various protei