5S rRNA binding proteins from the hyperthermophilic archaeon, Pyrococcus furiosus

FEBS Letters

Itoh, Takuzi²  Furumoto, Hiromi²  Taguchi, Atsuo²  Itoh, Takashi¹  Morinaga, Tsutomu² 

[1] Japan Collection of Microorganisms, The Institute of Physical and Chemical Research (RIKEN), Hirosawa, Wako City 351-0198, Japan;School of Bioresources, Hiroshima Prefectural University, Shobara City, Hiroshima 727-0023, Japan

关键词: 5S rRNA;    RNA-binding;    Ribosomal protein;    Archaea;    Pyrococcus furiosus;    rp;    ribosomal protein;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(00)02293-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown