Isolation and characterization of a growth-cycle-reflecting, high-molecular-weight protein associated with Escherichia coli ribosomes.
A high-molecular-weight, acidic protein, acidic protein whose amount per ribosomal particle depends on the growth cycle is shown to be associated with Escherichia coli ribosomes. The protein is associated with ribosomes from cells harvested at different phases of the growth cycle, but a large increase in its amount is seen with ribosomes from post-exponential phase cells. The protein is only slightly washed off the ribosomes by 1 M NH4CL. When ribosomes are dissociated it remains entirely with the 30-S subunits. We have purified the protein to homogeneity. It has a molecular weight of 70 000 and its amino acid composition showed some resemblance to that of ribosomal protein S1. However, the two proteins ar-shown variation in the acetylation of L12 during the growth cycle, indicated that certain proteins of (or associated with) E. coli ribosmes may carry specific biochemical roles connected with cellular adaption toward the stationary phase.
D000596:Amino Acids / Q000032:analysis; D049148:Aminoacylation; D002455:Cell Division; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D008970:Molecular Weight; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D000596:Amino Acids; D012269:Ribosomal Proteins