Kushiro M, Shimizu M, Tomita K
Facility of Pharmaceutical Sciences, Osaka University, Japan.
Eur J Biochem. 1987 Dec 30;170(1-2):93-8. doi: 10.1111/j.1432-1033.1987.tb13671.x.
The tuf gene, which encodes the elongation factor Tu (EF-Tu) of Thermus thermophilus HB8, and its flanking regions were cloned and sequenced. The gene encoding EF-G was found upstream of the 5' end of the tuf gene. The tuf gene of T. thermophilus HB8 had a very high G + C content and 84.5% of the third base in codon usage was either G or C. The deduced primary structure of the EF-Tu was composed of 405 amino acid residues with a Mr = 44658. A comparison of the amino acid sequence of EF-Tu from T. thermophilus HB8 with those of Escherichia coli and Saccharomyces cerevisiae mitochondria showed a very high sequence homology (65-70%). Two Cys residues out of the three found in E. coli EF-Tu had been replaced with Val in T. thermophilus HB8 EF-Tu. An extra amino acid sequence of ten residues, consisting predominantly of basic amino acids (Met-182-Gly-191), which does not occur in EF-Tu of E. coli, was found in T. thermophilus HB8.
编码嗜热栖热菌HB8延伸因子Tu(EF-Tu)的tuf基因及其侧翼区域被克隆并测序。发现编码EF-G的基因位于tuf基因5'端的上游。嗜热栖热菌HB8的tuf基因具有非常高的G + C含量,密码子使用中84.5%的第三位碱基为G或C。推导的EF-Tu一级结构由405个氨基酸残基组成,Mr = 44658。嗜热栖热菌HB8的EF-Tu氨基酸序列与大肠杆菌和酿酒酵母线粒体的EF-Tu氨基酸序列比较显示出非常高的序列同源性(65 - 70%)。在嗜热栖热菌HB8的EF-Tu中,大肠杆菌EF-Tu中发现的三个半胱氨酸残基中的两个被缬氨酸取代。在嗜热栖热菌HB8中发现了一个额外的由十个残基组成的氨基酸序列,主要由碱性氨基酸组成(Met-182-Gly-191),这在大肠杆菌的EF-Tu中不存在。