Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Helix bundle loops determine whether histidine kinases autophosphorylate in cis or in trans.

Journal of molecular biology - 12 Apr 2013

Ashenberg Orr, Keating Amy E, Laub Michael T

Abstract excerpt

Bacteria frequently use two-component signal transduction pathways to sense and respond to environmental and intracellular stimuli. Upon receipt of a stimulus, a homodimeric sensor histidine kinase autophosphorylates and then transfers its phosphoryl group to a cognate response regulator. The autophosphorylation of histidine kinases has been reported to occur both in cis and in trans, but the molecular...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Outer Membrane Proteins
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence Resonance Energy Transfer

Share to Histidine Kinase

Share to Luminescent Proteins

Share to Multienzyme Complexes

Share to Protein Kinases

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 23333741
DOI: 10.1016/j.jmb.2013.01.011
PMCID: PMC3636764

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Helix bundle loops determine whether histidine kinases autophosphorylate in cis or in trans.PMID 23333741Read ↗

A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases.Semantic proximity Read ↗

Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases.Semantic proximity Read ↗

Routes of phosphoryl group transfer during signal transmission and signal decay in the dimeric sensor histidine kinase ArcB.Semantic proximity Read ↗

A link between dimerization and autophosphorylation of the response regulator PhoB.Semantic proximity Read ↗

The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm.Semantic proximity Read ↗

Phosphatase activity of histidine kinase EnvZ without kinase catalytic domain.Semantic proximity Read ↗

Allosteric mechanism of signal transduction in the two-component system histidine kinase PhoQ.Semantic proximity Read ↗

Artificial signaling in mammalian cells enabled by prokaryotic two-component system.Semantic proximity Read ↗

Structural insights into the signal transduction mechanism of the K+-sensing two-component system KdpDE.Semantic proximity Read ↗

<i>In vivo</i> cross-linking and transmembrane helix dynamics support a bidirectional non-piston model of signaling within <i>E. coli</i> EnvZSemantic proximity Read ↗

Validation of Cis and Trans Modes in Multistep Phosphotransfer Signaling of Bacterial Tripartite Sensor Kinases by Using Phos-Tag SDS-PAGE.Semantic proximity Read ↗

Structural plasticity and catalysis regulation of a thermosensor histidine kinase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.