ArticleProtein science : a publication of the Protein Society2004
Accessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residues.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 23 citations in OpenAlex.
- Bacterial Chemoreceptors Transmit Stimulus Signals Through Coupled Entropic Switches.Journal of molecular biology · 2026Article
- Spatial Restrictions in Chemotaxis Signaling Arrays: A Role for Chemoreceptor Flexible Hinges across Bacterial Diversity.International journal of molecular sciences · 2019Article
- Penetration into membrane of amino-terminal region of SecA when associated with SecYEG in active complexes.Protein science : a publication of the Protein Society · 2018Article
- Evidence for a Helix-Clutch Mechanism of Transmembrane Signaling in a Bacterial Chemoreceptor.Journal of molecular biology · 2016Article
- Differential backbone dynamics of companion helices in the extended helical coiled-coil domain of a bacterial chemoreceptor.Protein science : a publication of the Protein Society · 2015Article
- A Trigger Residue for Transmembrane Signaling in the Escherichia coli Serine Chemoreceptor.Journal of bacteriology · 2015Article
- Forcing the issue: aromatic tuning facilitates stimulus-independent modulation of a two-component signaling circuit.ACS synthetic biology · 2015Article
- Differential repositioning of the second transmembrane helices from E. coli Tar and EnvZ upon moving the flanking aromatic residues.Biochimica et biophysica acta · 2015Article
- Employing aromatic tuning to modulate output from two-component signaling circuits.Journal of biological engineering · 2015Article
- The role of membrane-mediated interactions in the assembly and architecture of chemoreceptor lattices.PLoS computational biology · 2014Article
- Influence of membrane lipid composition on a transmembrane bacterial chemoreceptor.The Journal of biological chemistry · 2012Article
- Mutational analysis of the control cable that mediates transmembrane signaling in the Escherichia coli serine chemoreceptor.Journal of bacteriology · 2011Article
- Transmembrane signaling of chemotaxis receptor tar: insights from molecular dynamics simulation studies.Biophysical journal · 2011Article
- Polar chemoreceptor clustering by coupled trimers of dimers.Biophysical journal · 2009Article
- Bacterial chemoreceptors: high-performance signaling in networked arrays.Trends in biochemical sciences · 2008Review
- The control of transmembrane helix transverse position in membranes by hydrophilic residues.Journal of molecular biology · 2007Article
- Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli.Journal of bacteriology · 2006Article
- Diagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identity.Protein science : a publication of the Protein Society · 2006Article
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2 authors at 1 institution in 1 country.
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Abstract
Two hydrophobic sequences, 24 and 30 residues long, identify the membrane-spanning segments of chemoreceptor Trg from Escherichia coli. As in other related chemoreceptors, these helical sequences are longer than the minimum necessary for an alpha-helix to span the hydrocarbon region of a biological membrane. Thus, the specific positioning of the segments relative to the hydrophobic part of the membrane cannot be deduced from sequence alone. With the aim of defining the positioning for Trg experimentally, we determined accessibility of a hydrophilic sulfhydryl reagent to cysteines introduced at each position within and immediately outside the two hydrophobic sequences. For both sequences, there was a specific region of uniformly low accessibility, bracketed by regions of substantial accessibility. The two low-accessibility regions were each 19 residues long and were in register in the three-dimensional organization of the transmembrane domain deduced from independent data. None of the four hydrophobic-hydrophilic boundaries for these two membrane-embedded sequences occurred at a charged residue. Instead, they were displaced one to seven residues internal to the charged side chains bracketing the extended hydrophobic sequences. Many hydrophobic sequences, known or predicted to be membrane-spanning, are longer than the minimum necessary helical length, but precise membrane boundaries are known for very few. The cysteine-accessibility approach provides an experimental strategy for determining those boundaries that could be widely applicable.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.