Non-stressful death of 23S rRNA mutant G2061C defective in puromycin reaction

Petr V. Sergiev, Dmitry V. Lesnyak, Dmitry E. Burakovsky, Maxim Svetlov, Vyacheslav A. Kolb, Marina V. Serebryakova, Irina A. Demina, Vadim M. Govorun, Olga A. Dontsova, Alexey A. Bogdanov

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


Catalysis of peptide bond formation in the peptidyl transferase center is a major enzymatic activity of the ribosome. Mutations limiting peptidyl transferase activity are mostly lethal. However, cellular processes triggered by peptidyl transferase deficiency in the bacterial cell are largely unknown. Here we report a study of the lethal G2061C mutant of Escherichia coli 23S ribosomal RNA (rRNA). The G2061C mutation completely impaired the puromycin reaction and abolished formation of the active firefly luciferase in an in vitro translation system, while poly(U)- and short synthetic mRNA-directed peptidyl transferase reaction with aminoacylated tRNAs in vitro was seemingly unaffected. Study of the cellular proteome upon expression of the 23S rRNA gene carrying the G2061C mutation compared to cells expressing wild-type 23S rRNA gene revealed substantial differences. Most of the observed effects in the mutant were associated with reduced expression of stress response proteins and particularly proteins associated with the ppGpp-mediated stringent response.

Original languageEnglish
Pages (from-to)656-667
Number of pages12
JournalJournal of Molecular Biology
Issue number5
Publication statusPublished - 9 Mar 2012
Externally publishedYes


  • peptidyl transferase
  • ppGpp
  • ribosome
  • site-directed mutagenesis
  • stress response


Dive into the research topics of 'Non-stressful death of 23S rRNA mutant G2061C defective in puromycin reaction'. Together they form a unique fingerprint.

Cite this