scholarly journals Gating of CFTR by the STAS domain of SLC26 transporters

2004 ◽  
Vol 6 (4) ◽  
pp. 343-350 ◽  
Author(s):  
Shigeru B.H. Ko ◽  
Weizhong Zeng ◽  
Michael R. Dorwart ◽  
Xiang Luo ◽  
Kil Hwan Kim ◽  
...  
Keyword(s):  
Stas Domain

scholarly journals Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c fromMycobacterium tuberculosis

2010 ◽  
Vol 286 (10) ◽  
pp. 8534-8544 ◽  
Author(s):  
Alok K. Sharma ◽  
Liwen Ye ◽  
Christina E. Baer ◽  
Kumaran Shanmugasundaram ◽  
Tom Alber ◽  
...  
Keyword(s):  
Solution Structure ◽  
Nucleotide Binding ◽  
Guanine Nucleotide ◽  
Stas Domain ◽  
Guanine Nucleotide Binding

scholarly journals Novel Human Polymorphisms Define a Key Role for the SLC26A6-STAS Domain in Protection From Ca2+-Oxalate Lithogenesis

2020 ◽  
Vol 11 ◽  
Author(s):  
Liana Shimshilashvili ◽  
Sara Aharon ◽  
Orson W. Moe ◽  
Ehud Ohana
Keyword(s):  
Stas Domain

scholarly journals Structure of a SLC26 Anion Transporter STAS Domain in Complex with Acyl Carrier Protein: Implications for E. coli YchM in Fatty Acid Metabolism

Structure ◽  
2010 ◽  
Vol 18 (11) ◽  
pp. 1450-1462 ◽  
Author(s):  
Mohan Babu ◽  
Jack F. Greenblatt ◽  
Andrew Emili ◽  
Natalie C.J. Strynadka ◽  
Reinhart A.F. Reithmeier ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Metabolism ◽  
Acid Metabolism ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
E Coli ◽  
Anion Transporter ◽  
Stas Domain

scholarly journals Structural characterization of the STAS domain of prestin

2015 ◽  
Vol 71 (a1) ◽  
pp. s252-s252
Author(s):  
Elisa Costanzi ◽  
Graziano Lolli ◽  
Elisa Pasqualetto ◽  
Greta Bonetto ◽  
Roberto Battistutta
Keyword(s):  
Structural Characterization ◽  
Stas Domain

scholarly journals STAS Domain Only Proteins in Bacterial Gene Regulation

2021 ◽  
Vol 11 ◽  
Author(s):  
Brian E. Moy ◽  
J. Seshu
Keyword(s):  
Gene Expression ◽  
Sigma Factor ◽  
Environmental Changes ◽  
Vibrio Fischeri ◽  
Regulatory System ◽  
Sigma Factors ◽  
Amino Acid Sequences ◽  
Bacterial Gene ◽  
Anion Transporters ◽  
Stas Domain

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.

scholarly journals Localization of Slc26a9 and role of the STAS domain

2006 ◽  
Vol 20 (5) ◽  
Author(s):  
Aleksandra Sindic ◽  
Consuelo Plata ◽  
Caroline R. Sussman ◽  
David B. Mount ◽  
Min‐Hwang Chang ◽  
...  
Keyword(s):  
Stas Domain

scholarly journals STAS Domain Structure and Function

2011 ◽  
Vol 28 (3) ◽  
pp. 407-422 ◽  
Author(s):  
Alok K. Sharma ◽  
Alan C. Rigby ◽  
Seth L. Alper
Keyword(s):  
Domain Structure ◽  
Structure And Function ◽  
Stas Domain ◽  
And Function

scholarly journals The STAS domain of mammalian SLC26A5 prestin harbours an anion-binding site

2016 ◽  
Vol 473 (4) ◽  
pp. 365-370 ◽  
Author(s):  
Graziano Lolli ◽  
Elisa Pasqualetto ◽  
Elisa Costanzi ◽  
Greta Bonetto ◽  
Roberto Battistutta
Keyword(s):  
Binding Site ◽  
Anion Transport ◽  
Anion Binding ◽  
Stas Domain

The STAS domain of mammalian prestin harbours an anion-binding site absent from non-mammalian homologues. This is correlated to different prestin functions, full anion transport in non-mammals and incomplete transport coupled to electromotility and a mechanically amplified hearing process in mammals.

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