Mutational alterations in 50 proteins of the Escherichia coli ribosome.
A strain of Escherichia coli, VT, which spontaneously gives rise to mutations in many ribosomal proteins, has been used in conjunction with chemical mutagenesis and varying the subsequent incubation temperature to select mutants which have alterations in every ribosomal protein amenable to analysis of 70 S proteins on two-dimensional polyacrylamide gels under standard conditions. Alterations have been detected in 50 ribosomal proteins, namely in 20 from the small and in 30 from the large subunit. This is the most complete set of mutants with altered ribosomal proteins described so far. The difficulty until recently in obtaining mutations in most ribosomal proteins arises not because they are lethal, as has often been supposed, but because of the lack of a suitable selection heretofore.
D004587:Electrophoresis, Agar Gel; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics*; D005821:Genetic Techniques; D008769:Methylnitronitrosoguanidine / Q000494:pharmacology; D009154:Mutation; D011498:Protein Precursors / Q000235:genetics*; D012269:Ribosomal Proteins / Q000235:genetics*; D012641:Selection, Genetic
D011498:Protein Precursors; D012269:Ribosomal Proteins; D008769:Methylnitronitrosoguanidine