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. 1971 Sep;68(9):2263–2267. doi: 10.1073/pnas.68.9.2263

Alteration of a 30S Ribosomal Protein Accompanying the ram Mutation in Escherichia coli

Robert A Zimmermann 1,*, Robert T Garvin 1, Luigi Gorini 1,†
PMCID: PMC389397  PMID: 4943794

Abstract

The functional peculiarities of ram mutants correlate with an observed alteration in chromatographic mobility of P4a, a specific protein of the 30S ribosomal subunit. This finding is supported by ribosomal reconstitution experiments. These facts, together with the known location of the ram mutational site in the vicinity of other 30S genetic determinants, suggest that ram is the structural gene for P4a.

The known contrasting roles of ram and strA in determining translational efficiency require that the function of P4a should be explained in relation to P10 (the 30S-subunit protein defined by strA). One consequence of altering P4a, a key protein in ribosome assembly, might be to change the interaction of P10 with the 30S subunit. The functional interrelationship of P4a and P10 is discussed in terms of the possible roles of these two proteins in regulating access of tRNA molecules to the decoding site.

Keywords: split proteins, core proteins, misreading, translational restriction

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Selected References

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