In this study, a comparative analysis of the codon usage bias was performed in Aeropyrum pernix K1 and two other phylogenetically related Crenarchaeota microorganisms （i.e., Pyrobaculum aerophilum str. IM2 and Sulfol...In this study, a comparative analysis of the codon usage bias was performed in Aeropyrum pernix K1 and two other phylogenetically related Crenarchaeota microorganisms （i.e., Pyrobaculum aerophilum str. IM2 and Sulfolobus acidocaldarius DSM 639）. The results indicated that the synonymous codon usage in A. pernix K1 was less biased, which was highly correlated with the GC3s value. The codon usage patterns were phylogenetically conserved among these Crenarchaeota microorganisms. Comparatively, it is the species function rather than the gene function that determines their gene codon usage patterns. A. pernix K1, P. aerophilum str. IM2, and S. acidocaldarius DSM 639 live in differently extreme conditions. It is presumed that the hving environment played an important role in determining the codon usage pattern of these microorganisms. Besides, there was no strain-specific codon usage among these microorganisms. The extent of codon bias in A. pernix K1 and S. acidocaldarius DSM 639 were highly correlated with the gene expression level, but no such association was detected in P. aerophilum str. IM2 genomes.展开更多
The gene of enzyme（Ape1547） was cloned from hyperthermophilic archaeon Aeropyrum pernix K1 and expressed in Escherichia coil.The effect of calcium cation on the properties of Ape1547 was studied.Ape1547 exhibits bot...The gene of enzyme（Ape1547） was cloned from hyperthermophilic archaeon Aeropyrum pernix K1 and expressed in Escherichia coil.The effect of calcium cation on the properties of Ape1547 was studied.Ape1547 exhibits both peptidase activity and esterase activity.The fluorescence spectrum shows that calcium cation quenches the fluorescence of the enzyme through static quenching mechanism,indicating that calcium cation was bound to the enzyme.Based on the study of calcium cation on CD ellipticity of Ape1547 by circular dichroism,we concluded that the change of enzyme structure induced by calcium cation may be responsible for the change of enzyme activity.Calcium cation has dual effects on Ape1547：it could activate the enzyme activity when its concentration was 0.1 mol/L,and the enzyme had the highest activity;however,when its concentration was higher than 0.2 mol/L,the enzyme activity was inhibited.The results indicate that the activity center of peptidase activity might involve more amino acid residues than that of esterase activity.展开更多
A primitive orthorhombic crystal form of acylamino acid releasing enzyme/lipase (APE1547) from hyperthermophilic archaeon Aeropyrum pernix strain K1 has been obtained at 291 K. The diffraction pattern of the crystal e...A primitive orthorhombic crystal form of acylamino acid releasing enzyme/lipase (APE1547) from hyperthermophilic archaeon Aeropyrum pernix strain K1 has been obtained at 291 K. The diffraction pattern of the crystal extends to 0.27 nm resolution at 100 K using Cu Ka radiation. The crystal belongs to the space group P212121 with unit cell dimensions of a = 6.399, b = 10.439 and c = 16.953 nm. The presence of two molecules per asymmetric unit gives a crys-tal volume per protein mass (Vm) of 0.0022 nm3 Da-1 and a solvent content of 43% by volume. A full set of X-ray dif-fraction data were collected to 0.3 nm from the native crys-tal.展开更多
基金The work is supported by National Natural Science Foundation of China (No. 60121101).
文摘In this study, a comparative analysis of the codon usage bias was performed in Aeropyrum pernix K1 and two other phylogenetically related Crenarchaeota microorganisms （i.e., Pyrobaculum aerophilum str. IM2 and Sulfolobus acidocaldarius DSM 639）. The results indicated that the synonymous codon usage in A. pernix K1 was less biased, which was highly correlated with the GC3s value. The codon usage patterns were phylogenetically conserved among these Crenarchaeota microorganisms. Comparatively, it is the species function rather than the gene function that determines their gene codon usage patterns. A. pernix K1, P. aerophilum str. IM2, and S. acidocaldarius DSM 639 live in differently extreme conditions. It is presumed that the hving environment played an important role in determining the codon usage pattern of these microorganisms. Besides, there was no strain-specific codon usage among these microorganisms. The extent of codon bias in A. pernix K1 and S. acidocaldarius DSM 639 were highly correlated with the gene expression level, but no such association was detected in P. aerophilum str. IM2 genomes.
基金Supported by the National Natural Science Foundation of China(Nos.30400081 and 20772046)
文摘The gene of enzyme（Ape1547） was cloned from hyperthermophilic archaeon Aeropyrum pernix K1 and expressed in Escherichia coil.The effect of calcium cation on the properties of Ape1547 was studied.Ape1547 exhibits both peptidase activity and esterase activity.The fluorescence spectrum shows that calcium cation quenches the fluorescence of the enzyme through static quenching mechanism,indicating that calcium cation was bound to the enzyme.Based on the study of calcium cation on CD ellipticity of Ape1547 by circular dichroism,we concluded that the change of enzyme structure induced by calcium cation may be responsible for the change of enzyme activity.Calcium cation has dual effects on Ape1547：it could activate the enzyme activity when its concentration was 0.1 mol/L,and the enzyme had the highest activity;however,when its concentration was higher than 0.2 mol/L,the enzyme activity was inhibited.The results indicate that the activity center of peptidase activity might involve more amino acid residues than that of esterase activity.
基金This work was supported by the 73 Project (Grant No. G1999075602).
文摘A primitive orthorhombic crystal form of acylamino acid releasing enzyme/lipase (APE1547) from hyperthermophilic archaeon Aeropyrum pernix strain K1 has been obtained at 291 K. The diffraction pattern of the crystal extends to 0.27 nm resolution at 100 K using Cu Ka radiation. The crystal belongs to the space group P212121 with unit cell dimensions of a = 6.399, b = 10.439 and c = 16.953 nm. The presence of two molecules per asymmetric unit gives a crys-tal volume per protein mass (Vm) of 0.0022 nm3 Da-1 and a solvent content of 43% by volume. A full set of X-ray dif-fraction data were collected to 0.3 nm from the native crys-tal.
