Tail-Anchored Inner Membrane Protein ElaB Increases Resistance to Stress While Reducing Persistence in Escherichia coli
Abstract
Host-associated bacteria, such as Escherichia coli , often encounter various host-related stresses, such as nutritional deprivation, oxidative stress, and temperature shifts. There is growing interest in searching for small endogenous proteins that mediate stress responses. Here, we characterized the small C-tail-anchored inner membrane protein ElaB in E. coli . ElaB belongs to a class of tail-anchored inner membrane proteins with a C-terminal transmembrane domain but lacking an N-terminal signal sequence for membrane targeting. Proteins from this family have been shown to play vital roles, such as in membrane trafficking and apoptosis, in eukaryotes; however, their role in prokaryotes is largely unexplored. Here, we found that the transcription of elaB is induced in the stationary phase in E. coli and stationary-phase sigma factor RpoS regulates elaB transcription by binding to the promoter of elaB . Moreover, ElaB protects cells against oxidative stress and heat shock stress. However, unlike membrane peptide toxins TisB and GhoT, ElaB does not lead to cell death, and the deletion of elaB greatly increases persister cell formation. Therefore, we demonstrate that disruption of C-tail-anchored inner membrane proteins can reduce stress resistance; it can also lead to deleterious effects, such as increased persistence, in E. coli .
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- May 01, 2017
- Source ID
- 10.1128/jb.00057-17
Entities
People
- Baiyuan Li
- Jianyun Yao
- Thomas K. Wood
- Xiaoxiao Liu
- Xiaoxue Wang
- Yunxue Guo
Organizations
- Army Research Office
- China Postdoctoral Science Foundation
- National Natural Science Foundation of China
- National Science Foundation
- Pennsylvania State University
- University of Chinese Academy of Sciences