The effects of mutations in the rpmB,G operon of Escherichia coli on ribosome assembly and ribosomal protein synthesis.

The rpmB,G operon of Escherichia coli codes for proteins L28 and L33 of the larger (50S) ribosomal subunit. Strains with mutations in this operon can help define the roles of these proteins in ribosome synthesis and function. One such strain, BM108, makes neither protein and is unable to synthesize completed ribosomes; instead ribonucleoproteins accumulate, in the form of '30S material' and '47S particles'. However, when protein L28 is supplied from a plasmid, the growth rate, the kinetics of ribosome synthesis and the coordination of ribosomal protein synthesis are no different from that in wild-type organisms even though protein L33 is missing. This suggests that the latter protein can be redundant for ribosome synthesis and function. Another mutant strain, BM81, has a frameshift mutation that gives rise to an oversized protein L28. This mutant accumulates 30S material and 47S particles during slow exponential growth. The composition of the 47S particles from strains BM81, BM108 and a third mutant strain, TP28, suggests that their defining feature is the absence of L28; this is further evidence for an important role for this protein in ribosome assembly. Accumulation of ribonucleoproteins in strains BM81 and BM108 leads to some loss of the ordinarily precise coordination of synthesis of ribosomal proteins. We describe and discuss the characteristic features of this unbalanced synthesis.