Ribonuclease E strongly impacts bacterial adaptation to different growth conditions

RNA Biol. 2023 Jan;20(1):120-135. doi: 10.1080/15476286.2023.2195733.

Abstract

Adaptation of bacteria to changes in their environment is often accomplished by changes of the transcriptome. While we learned a lot on the impact of transcriptional regulation in bacterial adaptation over the last decades, much less is known on the role of ribonucleases. This study demonstrates an important function of the endoribonuclease RNase E in the adaptation to different growth conditions. It was shown previously that RNase E activity does not influence the doubling time of the facultative phototroph Rhodobacter sphaeroides during chemotrophic growth, however, it has a strong impact on phototrophic growth. To better understand the impact of RNase E on phototrophic growth, we now quantified gene expression by RNA-seq and mapped 5' ends during chemotrophic growth under high oxygen or low oxygen levels and during phototrophic growth in the wild type and a mutant expressing a thermosensitive RNase E. Based on the RNase E-dependent expression pattern, the RNAs could be grouped into different classes. A strong effect of RNase E on levels of RNAs for photosynthesis genes was observed, in agreement with poor growth under photosynthetic conditions. RNase E cleavage sites and 5' ends enriched in the rnets mutant were differently distributed among the gene classes. Furthermore, RNase E affects the level of RNAs for important transcription factors thus indirectly affecting the expression of their regulons. As a consequence, RNase E has an important role in the adaptation of R. sphaeroides to different growth conditions. [Figure: see text].

Keywords: RNA processing; RNase E; Rhodobacter; bacterial adaptation; photosynthesis genes; riboregulation; transcriptome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteria / metabolism
  • Bacterial Proteins* / genetics
  • Bacterial Proteins* / metabolism
  • Endoribonucleases* / genetics
  • Oxygen

Substances

  • ribonuclease E
  • Bacterial Proteins
  • Endoribonucleases
  • Oxygen

Grants and funding

Deutsche Forschungsgemeinschaft [Kl 561/41-1, RTG 2355]; IZKF at the University Würzburg [project Z-6]. Funding for open access charge: Deutsche Forschungsgemein-schaft/University of Giessen