Polyuridylic acid binding and translating by Escherichia coli ribosomes: Stimulation by Protein 1, inhibition by aurintricarboxylic acid

Moshe Tal, Michael Aviram, Adam Kanarek, Anna Weiss

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

Abstract

Prolonged dialysis of Escherichia coli ribosomes against low ionic strength buffer results in release of several acidic proteins, one of which is capable of interacting with poly(U) as well as augmenting its binding and translation by ribosomes. Its acidic nature, amino acid composition and molecular weight (65 000), identified it as one of the 30-S ribosomal proteins, namely Kurland's Protein 1, Wittman's Protein S1, Moore's Protein 13 or Nomura's P1. Aurintricarboxylic acid, which inhibits binding of poly(U) to ribosomes, has the same effect on binding of poly(U) to the pure Protein 1 preparation at a similar concentration. The possibility that Protein 1 comprises the active site for mRNA binding on the 30-S ribosome, or at least contributes to it, is discussed.

Original languageEnglish
Pages (from-to)381-392
Number of pages12
JournalBBA Section Nucleic Acids And Protein Synthesis
Volume281
Issue number3
DOIs
StatePublished - 27 Oct 1972
Externally publishedYes

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