Open AccessAlteration of a 30S Ribosomal Protein Accompanying the ram Mutation in Escherichia coli
Author(s) -
Robert A. Zimmermann,
Robert T. Garvin,
Luigi Gorini
Publication year - 1971
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.68.9.2263
Subject(s) - 30s , ribosomal protein , ribosome , protein subunit , biology , ribosomal rna , genetics , eukaryotic small ribosomal subunit , eukaryotic large ribosomal subunit , escherichia coli , mutant , transfer rna , mutation , computational biology , gene , rna
The functional peculiarities ofram 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 theram mutational site in the vicinity of other 30S genetic determinants, suggest thatram is the structural gene for P4a .The known contrasting roles ofram andstrA in determining translational efficiency require that the function of P4a should be explained in relation to P10 (the 30S-subunit protein defined bystrA ). 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.