Identification of three 30S proteins contributing to the ribosomal A site View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1972-09

AUTHORS

L. L. Randall-Hazelbauer, C. G. Kurland

ABSTRACT

When 30S ribosomal subunits from E. coli are incubated with unfractionated 30S protein, the protein synthetic activity of the ribosomes is enhanced. Part of this effect is due to the stimulation of mRNA binding by S1 (Van Duin and Kurland, 1970). In addition, three other proteins (S2, S3 and S14) increase the number of tRNA binding sites. The enhancing effect of S2, S3 and S14 on the tRNA binding capacity of the ribosomes is seen both in the presence and absence of T factor. S2, S3 and S14 do not seem to stimulate mRNA binding. The aminoacyl-tRNA bound in response to S2, S3 and S14 is associated with the 70S ribosome and it can donate amino acid residues for polypeptide synthesis. We conclude that S2, S3 and S14 are part of the 30S A site. More... »

PAGES

234-242

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00268887

DOI

http://dx.doi.org/10.1007/bf00268887

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005816286

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/4555677


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