HSP70 and ribosomal protein L2: novel 5S rRNA binding proteins in Escherichia coli

FEBS Letters

Aimi, Tadanori¹  Okada, Saori¹  Itoh, Takuzi¹  Okada, Tetsuji¹  Morinaga, Tsutomu¹ 

[1] School of Bioresources, Hiroshima Prefectural University, Shobara City, Hiroshima 727-0023, Japan

关键词: 5S rRNA;    RNA binding protein;    Ribosomal protein L2;    Heat shock protein;    HSP70;    Escherichia coli;   

DOI  :  10.1016/S0014-5793(00)02184-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A Northwestern analysis of Escherichia coli total proteins with radiolabeled 5S rRNA identified two novel 5S rRNA interacting proteins, a 70 kDa and a 37 kDa protein, and three ribosomal proteins reported on already. The N-terminal sequencing of the 70 kDa protein separated by SDS–PAGE from the high-salt-washed fraction of crude ribosome led to the discovery of a polypeptide identical in its first 10 amino acid residues to E. coli heat shock protein 70. The N-terminal eight amino acid sequence of the 37 kDa protein extracted from the high-salt-washed ribosome is identical to that of the ribosomal protein L2. In addition, the interaction of these proteins with 5S rRNA has been confirmed with gel mobility shift assays.

【 授权许可】

Unknown