2014
DOI: 10.1111/1574-6968.12385
|View full text |Cite
|
Sign up to set email alerts
|

Expression of theEscherichia coliompWcolicin S4 receptor gene is regulated by temperature and modulated by the H-NS and StpA nucleoid-associated proteins

Abstract: The OmpW family consists of a ubiquitous group of small outer membrane (OM) β-barrel proteins of Gram-negative bacteria with proposed roles in environmental adaptation but poorly understood mechanisms of expression. We report here that Escherichia coli K-12 OmpW contents are drastically modified by temperature changes compatible with the leap from the environment to warm-blooded hosts and/or vice versa. Thus, while OmpW is present in the OM of bacteria grown at 37 °C, it sharply disappears at 23 °C with the co… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

0
16
1

Year Published

2015
2015
2023
2023

Publication Types

Select...
7

Relationship

0
7

Authors

Journals

citations
Cited by 14 publications
(17 citation statements)
references
References 33 publications
0
16
1
Order By: Relevance
“…Asp116, His117 y Glu120 in that -helix form a charged patch showing a negative-positive-negative charge pattern that is totally complementary to the positive-negative-positive charge pattern of the -helix present in the receptor-binding domain of the bacteriocin colicin S4. This receptor-binding domain is unique, because it doesn't have a homologous sequence in other colicins, so colicin S4 is the only colicin able to bind to OmpW [25]. This fact is responsible for the high specificity of the biosensor method described in this study ( Figure 8).…”
Section: The Cellular Biomarkermentioning
confidence: 98%
“…Asp116, His117 y Glu120 in that -helix form a charged patch showing a negative-positive-negative charge pattern that is totally complementary to the positive-negative-positive charge pattern of the -helix present in the receptor-binding domain of the bacteriocin colicin S4. This receptor-binding domain is unique, because it doesn't have a homologous sequence in other colicins, so colicin S4 is the only colicin able to bind to OmpW [25]. This fact is responsible for the high specificity of the biosensor method described in this study ( Figure 8).…”
Section: The Cellular Biomarkermentioning
confidence: 98%
“…OmpA is an important outer membrane structural protein that maintains cell morphology and transfers hydrophilic compounds across the cell membrane (Danoff and Fleming 2011), and OmpC is the main cation-selective porin that enables the entry of small molecules into the bacteria (Baslé et al 2006;Joseph Sahaya Rajan et al 2015). In Gram-negative bacteria, OmpW encodes a small β-sheet membrane protein that allows the bacteria to adapt to environmental changes (Brambilla et al 2014), while the mechanism that controls OmpX expression is not clear. The levels of the mRNAs that encode these four proteins increased with the enhanced expression of rpoE during the early stage of induction (about 10 to 15 h) in the fermentation culture of W3110/pBZ001.…”
Section: The Stress Response and σ E -Dependent Cell Lysis In W3110/pmentioning
confidence: 99%
“…Haemorrhagic septicaemia has an extensive distribution world-wide especially in Africa and South East Asia. It is known to be associated with the localisation of bacteria in the tonsils of living buffalo, showing that animals can become transporters [4].…”
Section: Introductionmentioning
confidence: 99%