[Correlation analysis of (G + C)% of coding sequence and thermostability of xylose isomerase of thermophiles].
Statistical analysis about amino acids and coding sequence of xylose isomerase were performed in a number of thermophiles and mesophiles. It was found that there are correlations between the (G + C)% of the coding sequence and that of 1st, 2nd and 3rd position of the code of amino acids. There were also positive (for hydrophobic amino acids) and negative (for hydrophilic amino acids) correlation between the content of individual amino acids in the enzyme protein and the (G + C)% of their respective coding sequence. It speaks for the notion that high content of (G + C) in the coding sequence tends to increase the thermostability of the corresponding protein. The results in the statistical analysis of amino acid substitutions leading to change in thermostability of the protein may also be interpreted in the same way. An increase in the (G + C)% of DNA of a bacterium can therefore not only increase the thermostability of DNA itself but its proteins as well. Evolutionary consequence concerning thermophily and coding system are discussed.
Zhu
W
W
Institute of Genetics Univ. Fudan State Key Laboratory of Genetic Engineering, Shanghai.
Zheng
Z H
ZH
Yuan
Y Z
YZ
Zhou
Z X
ZX
Mao
Y M
YM
D019747:Aldose-Ketose Isomerases / Q000737:chemistry / Q000235:genetics*; D020029:Base Pairing; D004795:Enzyme Stability; D006358:Hot Temperature
D019747:Aldose-Ketose Isomerases; C023298:xylose isomerase