HSP70 and ribosomal protein L2: novel 5S rRNA binding proteins in Escherichia coli.
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.
Okada
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School of Bioresources, Hiroshima Prefectural University, Shobara City, Hiroshima 727-0023, Japan.
Okada
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Aimi
T
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Morinaga
T
T
Itoh
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T
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry*; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry; D012341:RNA, Ribosomal, 5S / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism
D018840:HSP70 Heat-Shock Proteins; D010446:Peptide Fragments; D012341:RNA, Ribosomal, 5S; D012269:Ribosomal Proteins; C029466:ribosomal protein L2