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Ribosomal proteins: XLIII. In vivo assembly of Escherichia coli ribosomal proteins
Authors:Knud H Niebhaus  Karin Bordasch  Heide E Homann
Institution:Max-Planck-Institut für Molekulare Genetik, Abt. Wittmann Berlin-Dahlem, Germany
Abstract:Isolation of ribosomal precursors from Escherichia coli K12 is described. The RNA and protein content of the precursor particles was determined.One physiologically stable precursor was found for the 30 S subunit. The assembly scheme is as follows: p16 S RNA + 9 proteins → p30 S (“21 S” precursor) p30 S + 12 proteins → 30 S subunit where p is precursor.Each of the two precursors for the 50 S subunit, P150 S and p250 S (“32 S” and “43 S” precursors, respectively), contains p5 S + p23 S RNA's in a 1:1 molar ratio. The assembly scheme is as follows: p23 S RNA + p5 S RNA + 16 or 17 proteins → p150 S
/></figure> In contrast to the p<sub>2</sub>50 S precursor the p<sub>1</sub>50 S precursor is not similar to any core particles, which were obtained by treating 50 S subunits with different concentrations of LiCl or CsCl.The precursors p30 S and p<sub>2</sub>50 S can be converted into active 30 S and 50 S sub-units, respectively, by incubation at 42 °C in the presence of ribosomal proteins and under RNA methylating conditions.</td>
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