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  STAC: A New Domain Associated with Transmembrane Solute Transport and Two-Component Signal Transduction Systems

Korycinski, M., Albrecht, R., Ursinus, A., Hartmann, M., Coles, M., Martin, J., et al. (2015). STAC: A New Domain Associated with Transmembrane Solute Transport and Two-Component Signal Transduction Systems. Journal of Molecular Biology, 427(20), 3327-3339. doi:10.1016/j.jmb.2015.08.017.

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Korycinski, M1, Author           
Albrecht, R1, 2, Author           
Ursinus, A1, 3, Author           
Hartmann, MD1, 2, Author           
Coles, M1, 4, Author           
Martin, J1, 3, Author           
Dunin-Horkawicz, S1, Author           
Lupas, AN1, Author           
Affiliations:
1Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375791              
2Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477392              
3Protein Folding, Unfolding and Degradation Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477400              
4Transmembrane Signal Transduction Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3477410              

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 Abstract: Transmembrane receptors are integral components of sensory pathways in prokaryotes. These receptors share a common dimeric architecture, consisting in its basic form of an N-terminal extracellular sensor, transmembrane helices, and an intracellular effector. As an exception, we have identified an archaeal receptor family--exemplified by Af1503 from Archaeoglobus fulgidus--that is C-terminally shortened, lacking a recognizable effector module. Instead, a HAMP domain forms the sole extension for signal transduction in the cytosol. Here, we examine the gene environment of Af1503-like receptors and find a frequent association with transmembrane transport proteins. Furthermore, we identify and define a closely associated new protein domain family, which we characterize structurally using Af1502 from A. fulgidus. Members of this family are found both as stand-alone proteins and as domains within extant receptors. In general, the latter appear as connectors between the solute carrier 5 (SLC5)-like transmembrane domains and two-component signal transduction (TCST) domains. This is seen, for example, in the histidine kinase CbrA, which is a global regulator of metabolism, virulence, and antibiotic resistance in Pseudomonads. We propose that this newly identified domain family mediates signal transduction in systems regulating transport processes and name it STAC, for SLC and TCST-Associated Component.

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 Dates: 2015-10
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: DOI: 10.1016/j.jmb.2015.08.017
PMID: 26321252
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Title: Journal of Molecular Biology
  Other : JMB
  Abbreviation : J. Mol. Biol.
Source Genre: Journal
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Publ. Info: Elsevier
Pages: - Volume / Issue: 427 (20) Sequence Number: - Start / End Page: 3327 - 3339 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/0022-2836