Abstract
Escherichia coli spends a significant amount of energy to synthesize one (or more than one) enzyme which further spends energy in transferring nine methyl groups from S-adenosyl-methionine (SAM) to ribosomal protein L11. Our current opinion is that spending this energy is meaningless, because an E. coli mutant (prmA1) completely lacks methylation of L11 while exhibiting no detectable deleterious phenotype (Colson and Smith, 1977). We summarize here some of the efforts made, using mutant prmA1, to unveil a function of L11 methylation. In addition we present preliminary results of a cloning project to further characterize the methylating enzyme(s) of L11.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
ALIX J.H., HAYES D., LONTIE J.F., COLSON C., GLATIGNY A. & LEDERER F. (1979). Methylated amino acids in ribosomal proteins from Escherichia coli treated with ethionine and from a mutant lacking methylation of protein L11. Biochimie, 61, 671–679.
COLSON C. & SMITH H.O. (1977). Genetics of ribosomal protein methylation in Escherichia coli. I. A mutant deficient in methylation of protein L11. Molec. Gen. Genet., 154, 167–173.
COLSON C., LHOEST J. & URLINGS C. (1979). Genetics of ribosomal protein methylation in Escherichia coli. III. Map position of two genes, prmA and prmB, governing methylation of proteins L11 and L3. Molec. Gen. Genet., 169, 245–250.
ROHL R. & NIERHAUS K.H. (1979). Methylgroups of ribosomal protein L11 are not related to the synthesis of ppGpp. Molec. Gen. Genet., 170, 187–189.
STARK M.J.R., CUNDLIFFE E., DIJK J. & STOFFLER G. (1980). Functional homology between E. coli ribosomal protein L11 and B. megaterium protein BM-L11. Molec. Gen. Genet., 180, 11–15.
STOFFLER G., CUNDLIFFE E., STÖFFLER-MEILICKE M. & DABBS E. (1980). Mutants of Escherichia coli lacking ribosomal protein L11. J. Biol. Chem., 255, 10517–10522.
Author information
Authors and Affiliations
Copyright information
© 1982 The contributors
About this chapter
Cite this chapter
Lhoest, J. et al. (1982). Why is ribosomal protein L11 of Escherichia coli methylated?. In: Biochemistry of S-Adenosylmethionine and Related Compounds. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06343-7_11
Download citation
DOI: https://doi.org/10.1007/978-1-349-06343-7_11
Publisher Name: Palgrave Macmillan, London
Print ISBN: 978-1-349-06345-1
Online ISBN: 978-1-349-06343-7
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)