Ribosome profiling in Streptococcus pneumoniae reveals the role of methylation of 23S rRNA nucleotide G748 on ribosome stalling.
Source: NCBI BioProject (ID PRJDB10882)
Source: NCBI BioProject (ID PRJDB10882)
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Project name: Streptococcus pneumoniae
Description: Many nucleotides methylated post-transcriptionally by methyltransferases in 23S rRNA are clustered around the peptidyltransferase center (PTC) and the nascent peptidyl exit tunnel (NPET) located in 50S subunit of 70S ribosome. Biochemical interactions between the nascent peptide and the tunnel may stall the ribosome movement and thus affect the expression level of the protein being synthesized. However no studies have actually shown the role of NPET on the ribosome stalling using NPET mutant. By establishing the ribosome profiling assay in Streptococcus pneumoniae, we show for the first time that NPET mutant exhibits completely different ribosome occupancy compared to wild-type strain. Using RNA footprinting assay, we demonstrate that the observed change in the ribosome occupancy corresponds to the change in ribosome stalling. Further statistical analysis shows the short peptide sequences that cause ribosome stalling are specie-specific and evolutionary selected, and NPET structure is required to realize these characteristics. The reported results support the role of NPET on ribosome stalling. NPET structure is required to realize the specie-specific and evolutionary conserved ribosome stalling. These findings throw light on the role of the NPET structure on the translation process.
Data type: Transcriptome or Gene expression
Sample scope: Monoisolate
Organization: Laboratory of Microbiology and Immunology
Release date: 2020-12-26
Last updated: 2020-12-10