Methylation of ribosomal proteins during ribosome assembly in Escherichia coli.
In Escherichia coli, a number of ribosomal proteins are methylated. The time of methylation of L7 and L11 during ribosome assembly was studied. It was observed that the methylation of L7 could occur in the free protein stage. Both the 32S and 40S ribonucleoprotein intermediates also contained methylated L7 although the extent of methylation in these particles was not as high as in the free L7, the 45S or the 50S particles. Free L11 could also be partially methylated but the bulk of methylation of this protein was found in the 45S and the 50S particles. It was previously reported that the methylation of L7 is inversely proportional to the growth temperature (Chang 1978), we now show that once L7 is methylated at 25 degree, the methyl group is stable when the culture is shifted to 37 degree C. However, a partial turnover of the methyl group of L7 is observed when the methylated ribosome is chased at 25 degree C. On the other hand, the methyl groups of L11 appear to be stable at either 25 degree C or 37 degree C. We also observe that the extent of methylation of both L7 and L11 stays nearly constant during the cell growth cycle from early log to stationary phase.
D004926:Escherichia coli / Q000378:metabolism*; D005786:Gene Expression Regulation; D008745:Methylation; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D013997:Time Factors
D012269:Ribosomal Proteins