STAC--A New Domain Associated with Transmembrane Solute Transport and Two-Component Signal Transduction Systems
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 ...Continue Reading
References
Two WXXF-based motifs in NECAPs define the specificity of accessory protein binding to AP-1 and AP-2
HAMP domain-mediated signal transduction probed with a mycobacterial adenylyl cyclase as a reporter.
Citations
Transmembrane Signal Transduction in Two-Component Systems: Piston, Scissoring, or Helical Rotation?
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