Prestin and the good vibrations

Birke, Anna S; Javelle, Arnaud

doi:10.1042/bcj20160015

Cited by 2 publications

(1 citation statement)

References 16 publications

(27 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The role of the STAS domain in these SLC26/SulP has not been fully explored, but it has been suggested to be important for targeting proteins to the membrane ( Sharma et al., 2011 ; Compton et al., 2014 ). However, recent work has demonstrated that the STAS domain does not play a direct role in protein targeting in bacteria, but instead is required for protein stabilization and functionality ( Birke and Javelle, 2016 ; Lolli et al., 2016 ). In mammals, such as humans, SLC26 transporters play a diverse and critical role as anion exchangers, with three known mutations that can lead to early onset hereditary diseases: chondrodysplasias, chloride diarrhea, and deafness ( Compton et al., 2011 ; Alper and Sharma, 2013 ; Compton et al., 2014 ).…”

Section: Stas Domains As Part Of Slc26/sulp Familymentioning

confidence: 99%

STAS Domain Only Proteins in Bacterial Gene Regulation

Moy

Seshu

2021

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Sulfate Transport Anti-Sigma antagonist domains (Pfam01740) are found in all branches of life, from eubacteria to mammals, as a conserved fold encoded by highly divergent amino acid sequences. These domains are present as part of larger SLC26/SulP anion transporters, where the STAS domain is associated with transmembrane anchoring of the larger multidomain protein. Here, we focus on STAS Domain only Proteins (SDoPs) in eubacteria, initially described as part of the Bacillus subtilisRegulation of Sigma B (RSB) regulatory system. Since their description in B. subtilis, SDoPs have been described to be involved in the regulation of sigma factors, through partner-switching mechanisms in various bacteria such as: Mycobacterium. tuberculosis, Listeria. monocytogenes, Vibrio. fischeri, Bordetella bronchiseptica, among others. In addition to playing a canonical role in partner-switching with an anti-sigma factor to affect the availability of a sigma factor, several eubacterial SDoPs show additional regulatory roles compared to the original RSB system of B. subtilis. This is of great interest as these proteins are highly conserved, and often involved in altering gene expression in response to changes in environmental conditions. For many of the bacteria we will examine in this review, the ability to sense environmental changes and alter gene expression accordingly is critical for survival and colonization of susceptible hosts.

show abstract

Section: Stas Domains As Part Of Slc26/sulp Familymentioning

confidence: 99%

STAS Domain Only Proteins in Bacterial Gene Regulation

Moy

Seshu

2021

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

show abstract

The E. coli dicarboxylic acid transporters DauA act as a signal transducer by interacting with the DctA uptake system

Karinou

Hoskisson

Strecker

et al. 2017

Sci Rep

Self Cite

View full text Add to dashboard Cite

The Slc26A/SulP family of ions transporter is ubiquitous and widpsread in all kingdon of life. In E. coli, we have demonstrated that the Slc26 protein DauA is a C4-dicarboxilic acids (C4-diC) transporter active at acidic pH. The main C4-diC transporter active at pH7 is DctA and is induced by C4-diC via the DcuS/R two component system. DctA interacts with DcuS, the membrane embedded histidine kinase, to transfers DcuS to the responsive state, i.e. in the absence of DctA, DcuS is permanently “on”, but its activity is C4-diC-dependent when in complex with DctA. Using phenotypic characterization, transport assays and protein expression studies, we show that at pH7 full DctA production depends on the presence of DauA. A Bacterial Two Hybrid system indicates that DauA and the sensor complex DctA/DcuS physically interact at the membrane. Pull down experiments completed by co-purification study prove that DauA and DctA interact physically at the membrane. These data open a completely new aspect of the C4-diC metabolism in E. coli and reveals how the bacterial Slc26A uptake systems participate in multiple cellular functions. This constitutes a new example of a bacterial transporter that acts as a processor in a transduction pathway.

show abstract

Prestin and the good vibrations

Cited by 2 publications

References 16 publications

STAS Domain Only Proteins in Bacterial Gene Regulation

STAS Domain Only Proteins in Bacterial Gene Regulation

The E. coli dicarboxylic acid transporters DauA act as a signal transducer by interacting with the DctA uptake system

Contact Info

Product

Resources

About