4.6 Article

OmpA, a Common Virulence Factor, Is Under RNA Thermometer Control in Yersinia pseudotuberculosis

期刊

FRONTIERS IN MICROBIOLOGY
卷 12, 期 -, 页码 -

出版社

FRONTIERS MEDIA SA
DOI: 10.3389/fmicb.2021.687260

关键词

gene expression; thermosensor; RNA structure; pathogen; virulence; outer membrane protein; porin

资金

  1. German Research Foundation (DFG) [NA240/10-2]
  2. Open Access publication funds of the Ruhr-Universitat Bochum

向作者/读者索取更多资源

The study found evidence for a temperature-modulated RNA structure in the 5'-untranslated region of the OmpA transcript, supporting the hypothesis that melting of the RNA structure relieves translational repression. This allows for increased translation of the transcript at higher temperatures, with biochemical experiments showing that melting of the RNA structure permits ribosome binding to the 5'-UTR.
The outer membrane protein OmpA is a virulence factor in many mammalian pathogens. In previous global RNA structure probing studies, we found evidence for a temperature-modulated RNA structure in the 5'-untranslated region (5'-UTR) of the Yersinia pseudotuberculosis ompA transcript suggesting that opening of the structure at host-body temperature might relieve translational repression. Here, we support this hypothesis by quantitative reverse transcription PCR, translational reporter gene fusions, enzymatic RNA structure probing, and toeprinting assays. While ompA transcript levels decreased at 37 degrees C compared to 25 degrees C, translation of the transcript increased with increasing temperature. Biochemical experiments show that this is due to melting of the RNA structure, which permits ribosome binding to the 5'-UTR. A point mutation that locks the RNA structure in a closed conformation prevents translation by impairing ribosome access. Our findings add another common virulence factor to the growing list of pathogen-associated genes that are under RNA thermometer control.

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