Genetic analyses reveal distinct functional roles of Eut microcompartment shell proteins in ethanolamine metabolism in Salmonella
- 1CSIR-National Chemical Laboratory
Abstract
Ethanolamine utilization is an important metabolic capability of enteric bacteria and has been associated with bacterial fitness and adaptation within diverse host environment. In Salmonella enterica serovar Typhimurium, ethanolamine is metabolized within the bacterial microcompartment (Eut MCP), which is composed of five shell protein subunits. Deciphering how self-assembled shell proteins spatially organize the pathway, retain metabolic intermediates and create proper environment for catalysis is crucial for understanding role of Eut MCP in cellular metabolism and pathogenesis. Through genetic mutant construction, growth and metabolic assays, microscopy, and metabolite quantification, we demonstrate that each shell protein fulfills a distinct role to the functioning of the Eut MCP. Our findings provide mechanistic insights into the structural organization and functional dynamics of the bacterial microcompartment organelle.
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BibTeX
@misc{bhalerao2026genetic,
title = {{Genetic analyses reveal distinct functional roles of Eut microcompartment shell proteins in ethanolamine metabolism in Salmonella}},
author = {M. R. Bhalerao and A. A. Sutar and A. S. Davkhar and Y. D. Shinde and S. B. Agawane and C. Chowdhury},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.07.757396},
url = {https://www.biorxiv.org/content/10.64898/2026.10.07.757396v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Genetic analyses reveal distinct functional roles of Eut microcompartment shell proteins in ethanolamine metabolism in Salmonella
AU - M. R. Bhalerao
AU - A. A. Sutar
AU - A. S. Davkhar
AU - Y. D. Shinde
AU - S. B. Agawane
AU - C. Chowdhury
PY - 2026
DA - 2026/10/07
PB - bioRxiv
DO - 10.64898/2026.10.07.757396
UR - https://www.biorxiv.org/content/10.64898/2026.10.07.757396v1
AB - Ethanolamine utilization is an important metabolic capability of enteric bacteria and has been associated with bacterial fitness and adaptation within diverse host environment. In Salmonella enterica serovar Typhimurium, ethanolamine is metabolized within the bacterial microcompartment (Eut MCP), which is composed of five shell protein subunits. Deciphering how self-assembled shell proteins spatially organize the pathway, retain metabolic intermediates and create proper environment for catalysis is crucial for understanding role of Eut MCP in cellular metabolism and pathogenesis. Through genetic mutant construction, growth and metabolic assays, microscopy, and metabolite quantification, we demonstrate that each shell protein fulfills a distinct role to the functioning of the Eut MCP. Our findings provide mechanistic insights into the structural organization and functional dynamics of the bacterial microcompartment organelle.
ER -