Late consolidation of rRNA structure during co-transcriptional assembly in E. coli by time-resolved DMS footprinting.

ABSTRACT: The production of new ribosomes requires proper folding of the rRNA and the addition of more than 50 ribosomal proteins. The structures of some assembly intermediates have been determined by cryo-electron microscopy, yet these structures do not provide information on the folding dynamics of the rRNA. To visualize the changes in rRNA structure during ribosome assembly in E. coli cells, transcripts were pulse-labeled with 4-thiouridine and the structure of newly made rRNA probed at various times by dimethyl sulfate modification and mutational profiling sequencing (4U-DMS-MaPseq). The in-cell DMS modification patterns revealed that many long-range rRNA tertiary interactions and protein binding sites through the 16S and 23S rRNA remain partially unfolded 1.5 min after transcription. By

SUBMITTER: Hao Y 

PROVIDER: S-EPMC10802402 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature