Functional heterogeneity of the 30S ribosomal subunit of E. coli View Full Text


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Article Info

DATE

1970-06

AUTHORS

J. Van Duin, C. G. Kurland

ABSTRACT

When 30S ribosomal subunits from E. coli are incubated with poly U, two separable components are recovered by zonal centrifugation of the incubation mixture. The faster sedimenting component is an aggregate of 30S subunits and poly U, while the slower one corresponds to the 30S ribosomal subunit. One ribosomal protein, protein 30S-1 is predominantly present in the faster sedimenting aggregate. The amount of poly U-30S subunit complex formed in the incubation mixture is limited by the amount of protein 30S-1 present. Consequently the number of ribosomal binding sites available for Phe-tRNA is limited in a similar fashion by the presence of protein 30S-1. When 30S ribosomal subunits are reconstituted in the absence of protein 30S-1, very little poly U or Phe-tRNA binding capacity is manifest under our assay conditions. We conclude that protein 30S-1 is required for maximum capacity of ribosomes to bind mRNA. Since this protein is present only on a fraction of the ribosome at any one time, it must exchange from one ribosome to another during protein synthesis. More... »

PAGES

169-176

References to SciGraph publications

  • 1967-12. Ribosomal proteins in MOLECULAR GENETICS AND GENOMICS
  • 1970-06. Assembly Mapping of 30S Ribosomal Proteins from E. coli in NATURE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00269653

    DOI

    http://dx.doi.org/10.1007/bf00269653

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1016095600

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/4923592


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