Premium
Ribosome assembly in Escherichia coli strains lacking the RNA helicase DeaD/CsdA or DbpA
Author(s) -
Peil Lauri,
Virumäe Kai,
Remme Jaanus
Publication year - 2008
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2008.06523.x
Subject(s) - ribosome , rna helicase a , 50s , eukaryotic small ribosomal subunit , ribosomal rna , ribosome biogenesis , helicase , eukaryotic ribosome , biology , 23s ribosomal rna , rna , microbiology and biotechnology , peptidyl transferase , ribosomal protein , 30s , protein subunit , biochemistry , gene
Ribosome subunit assembly in bacteria is a fast and efficient process. Among the nonribosomal proteins involved in ribosome biogenesis are RNA helicases. We describe ribosome biogenesis in Escherichia coli strains lacking RNA helicase DeaD (CsdA) or DbpA. Ribosome large subunit assembly intermediate particles (40S) accumulate at 25 °C and at 37 °C in the absence of DeaD but not without DbpA. 23S rRNA is incompletely processed in the 40S and 50S particles of the DeaD − strain. Pulse labeling showed that the 40S particles are converted nearly completely into functional ribosomes. The rate of large ribosomal subunit assembly was reduced about four times in DeaD‐deficient cells. Functional activity tests of the ribosomal particles demonstrated that the final step of 50S assembly, the activation step, was affected when DeaD was not present. The results are compatible with the model that predicts multiple DeaD‐catalyzed structural transitions of the ribosome large subunit assembly.