| Literature DB >> 11094158 |
S Okada1, T Okada, T Aimi, T Morinaga, T Itoh.
Abstract
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.Entities:
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Year: 2000 PMID: 11094158 DOI: 10.1016/s0014-5793(00)02184-0
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124