Furumoto H, Taguchi A, Itoh T, Morinaga T, Itoh T
School of Bioresources, Hiroshima Prefectural University, Shobara City, Hiroshima, Japan.
FEBS Lett. 2000 Dec 15;486(3):195-9. doi: 10.1016/s0014-5793(00)02293-6.
A determination was made of the nucleotide sequence of the 2719 bp region of a ribosomal protein gene cluster (PfeL32-PfeL19-PfL18-PfS5-PfL30) containing a 5S rRNA binding protein L18 homolog of hyperthermophilic archaea Pyrococcus furiosus. The organization of the archaeal ribosomal protein gene cluster is similar to that in the spc-operon of Escherichia coli (L6-L18-S5-L30-L15) but has two additional genes, namely those encoding PfeL32 and PfeL19, which were identified as extra proteins that are apparently not present in bacterial E. coli. Using an inducible expression system, P. furiosus mature PfL18 protein and a mutant PfL18 with the basic N-terminal amino acid region deleted were produced in large amounts in E. coli and Northwestern analysis showed the N-terminal region of PfL18, including the conserved arginine-rich region, to have a significant role in 5S rRNA-PfL18 interaction.
测定了一个核糖体蛋白基因簇(PfeL32 - PfeL19 - PfL18 - PfS5 - PfL30)2719 bp区域的核苷酸序列,该基因簇包含嗜热古菌激烈火球菌(Pyrococcus furiosus)的5S rRNA结合蛋白L18的同源物。古菌核糖体蛋白基因簇的组织方式与大肠杆菌(Escherichia coli)的spc操纵子(L6 - L18 - S5 - L30 - L15)相似,但有两个额外的基因,即编码PfeL32和PfeL19的基因,它们被鉴定为在大肠杆菌中显然不存在的额外蛋白质。使用诱导表达系统,在大肠杆菌中大量产生了激烈火球菌成熟的PfL18蛋白和缺失碱性N端氨基酸区域的突变型PfL18,蛋白质印迹分析表明PfL18的N端区域,包括保守的富含精氨酸区域,在5S rRNA - PfL18相互作用中起重要作用。