1977
DOI: 10.1016/0014-5793(77)81039-9
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The interaction of transfer ribonucleic acid with 50 S ribosomal subunit proteins

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Cited by 16 publications
(9 citation statements)
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“…Under the experimental conditions, in agreement with [ 13,25,26], the immobilized intact 5 S RNA forms a complex with 3 ribosoma1 proteins: L5, L18 and L25. An identical result was obtained with the immobilized larger and smaller fragment, provided they were complemented with the free smaller or larger fragment, respectively (table 1).…”
Section: Resultssupporting
confidence: 72%
“…Under the experimental conditions, in agreement with [ 13,25,26], the immobilized intact 5 S RNA forms a complex with 3 ribosoma1 proteins: L5, L18 and L25. An identical result was obtained with the immobilized larger and smaller fragment, provided they were complemented with the free smaller or larger fragment, respectively (table 1).…”
Section: Resultssupporting
confidence: 72%
“…Various control experiments were detailed [3,4]. Besides those, one more criterion for specificity became evident from the fact that proteins bound to the immobilized tRNA can be washed out from the gel with a binding buffer solution containing excess tR.NA (data not shown).…”
Section: Resultsmentioning
confidence: 99%
“…In sum, spontaneous assembly of the tRNAprotein complex occurs when free ribosomal proteins are passed through a tRNA-Sepharose affinity column. This complex contains almost all the 30 S subunit proteins [3], identified at the ribosomal decoding site as well as 50 S subunit proteins [4] identified in or near to the peptidyl transferase center. Because of cooperativity observed between 30 S and 50 S subunit proteins during assembly (see above), we suggest that the complex represents an analogue of the subunits interface and is a compact, structurally integrated domain of ribosome, where both tRNA-protein and protein-protein interactions may be involved (discussed [4]).…”
Section: Resultsmentioning
confidence: 99%
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