Structural remodeling and activation of the hdeAB and proVWX operons in response to pH and salt stress
Abstract
Escherichia coli is highly sensitive to acid and osmotic stress but adapts by modulating the expression of stress-responsive genes. Nucleoid-associated proteins (NAPs) play key roles in DNA organization and sensing environmental changes. The histone-like nucleoid structuring protein H-NS is an NAP acting as a global regulator of stress genes. H-NS may alter local chromatin structure to modulate the expression of such genes in response to environmental stress. The H-NS homolog suppressor of td phenotype A (StpA) co-regulates several target genes, but its role is poorly defined. To investigate the regulatory interplay between these two proteins, we examined transcription, DNA binding, and chromatin structure at two regulated operons, hdeAB and proVWX , in E. coli following exposure to acid and salt shock. Our results show that H-NS senses pH and osmotic cues to remodel chromatin and relieve repression, while StpA—in part—compensates for H-NS loss, particularly at proVWX , highlighting a coordinated regulatory network.
Related
- A RecBCD-like enzyme regulates expression of bacterial defense operons in response to DNA damage
- Divergent evolutionary paths of vancomycin resistance operons reveal the transition from mobility to genomic stabilization in Enterococcus faecium
- Epigenome Alterations and 3D Chromatin Architecture Remodeling in Inflammatory Macrophage Activation under Diabetic Conditions
- Multi-omics profiling of the choroid plexus reveals developmental cellular remodeling, early immune gene activation, and epithelial cell heterogeneity
- Brain Landscape In Situ Crosslinking Mass Spectrometry (BLIS-XL-MS) Enables Global Analysis of Protein Structural Remodeling in the Brain
BibTeX
@article{ge2026structural,
title = {{Structural remodeling and activation of the hdeAB and proVWX operons in response to pH and salt stress}},
author = {Pingzhuang Ge and Fatema-Zahra M. Rashid and Luuk K.F. Gaarthuis and Marc K.M. Cajili and Minkang Tan and Baoxu Pang and Karin Schnetz and Remus T. Dame},
journal = {Cell Reports},
year = {2026},
month = oct,
doi = {10.1016/j.celrep.2026.118184},
url = {https://linkinghub.elsevier.com/retrieve/pii/S2211124726012635},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Structural remodeling and activation of the hdeAB and proVWX operons in response to pH and salt stress
AU - Pingzhuang Ge
AU - Fatema-Zahra M. Rashid
AU - Luuk K.F. Gaarthuis
AU - Marc K.M. Cajili
AU - Minkang Tan
AU - Baoxu Pang
AU - Karin Schnetz
AU - Remus T. Dame
PY - 2026
DA - 2026/10/30
JO - Cell Reports
DO - 10.1016/j.celrep.2026.118184
UR - https://linkinghub.elsevier.com/retrieve/pii/S2211124726012635
AB - Escherichia coli is highly sensitive to acid and osmotic stress but adapts by modulating the expression of stress-responsive genes. Nucleoid-associated proteins (NAPs) play key roles in DNA organization and sensing environmental changes. The histone-like nucleoid structuring protein H-NS is an NAP acting as a global regulator of stress genes. H-NS may alter local chromatin structure to modulate the expression of such genes in response to environmental stress. The H-NS homolog suppressor of td phenotype A (StpA) co-regulates several target genes, but its role is poorly defined. To investigate the regulatory interplay between these two proteins, we examined transcription, DNA binding, and chromatin structure at two regulated operons, hdeAB and proVWX , in E. coli following exposure to acid and salt shock. Our results show that H-NS senses pH and osmotic cues to remodel chromatin and relieve repression, while StpA—in part—compensates for H-NS loss, particularly at proVWX , highlighting a coordinated regulatory network.
SN - 2211-1247
ER -