The number of tRNA-binding sites on 80S ribosomes and their subunits

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Number of tRNA binding sites on 80 S ribosomes and their subunits.

The ability of rabbit liver ribosomes and their subunits to form complexes with different forms of tRNAPhe (aminoacyl-, peptidyl- and deacylated) was studied using the nitrocellulose membrane filtration technique. The 80 S ribosomes were shown to have two binding sites for aminoacyl- or peptidyl-tRNA and three binding sites for deacylated tRNA. The number of tRNA binding sites on 80 S ribosomes...

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tRNA binding sites on the subunits of Escherichia coli ribosomes.

Programmed 30 S subunits expose only one binding site, to which the different classes of tRNA (deacylated tRNAPhe, Phe-tRNAPhe, and N-acetylphenylalanyl (AcPhe)-tRNAPhe) bind with about the same affinity. Elongation factor Tu within the ternary complex does not contribute to the binding of Phe-tRNA. Binding of acylated or deacylated tRNA to 30 S depends on the cognate codon; nonprogrammed 30 S ...

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Interaction of tRNA with the A and P sites of rabbit-liver 80S ribosomes and their 40S subunits.

The interaction between tRNA and rabbit liver 80S ribosomes and 40S subunits was studied using a nitrocellulose membrane filtration technique. Binding of the different tRNA forms (aminoacyl-, peptidyl- or deacylated) to poly(U)-programmed 40S subunits and 80S ribosomes was found to be a cooperative process. The association constants of AcPhe-TRNA(Phe) for the A and P sites of 80S ribosomes and ...

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Proteins at the tRNA binding sites of Escherichia coli ribosomes.

p - Nitrophenylcarbamyl - phenylalanyl-tRNA binds to ribosomes in response to poly(U) and reacts with ribosomal proteins via covalent bond formation. Ribosomal proteins of Escherichia coli were characterized by two-dimensional gel electrophoresis and by reaction with specific antibodies. The affinity label is shown to react with the 50S proteins L27, L15, L2, L16, and L14. We therefore conclude...

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ژورنال

عنوان ژورنال: Biopolymers and Cell

سال: 1987

ISSN: 0233-7657,1993-6842

DOI: 10.7124/bc.0001e9