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Updated: Oct 10, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
Published on: March 8, 2024
HSP70 and ribosomal protein L2: novel 5S rRNA binding proteins in Escherichia coli
1School of Bioresources, Hiroshima Prefectural University, Shobara City, Hiroshima 727-0023, Japan.
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.
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