Signal Transmission through the HtrII Transducer Alters the Interaction of Two α-Helices in the HAMP Domain

Inoue, Kazuhide; Sasaki, Jun; Spudich, John L.; Terazima, Masahide

doi:10.1016/j.jmb.2007.12.026

Cited by 13 publications

(18 citation statements)

References 27 publications

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“…Prior disulfide mapping of the Salmonella typhimurium aspartate chemotaxis receptor HAMP domain by Butler and Falke (31) also showed only subtle shifts in residue accessibility following receptor activation, and previous study of SRII-HtrII complexes with truncation at different positions in the HAMP1 domain showed light-induced diffusion coefficient changes only when both AS1 and AS2 helices were present (32). These prior findings are consistent with signal transmission from a relative AS1-AS2 interface change.…”

Section: Discussionsupporting

confidence: 70%

HAMP Domain Signal Relay Mechanism in a Sensory Rhodopsin-Transducer Complex

Wang

Sasaki

Tsai

et al. 2012

Journal of Biological Chemistry

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Background: HAMP domains are four-helix bundles that transmit signals from receptor to output domains in signaling proteins/complexes. Results: Opposite stimulus-induced helix motions with opposite signal output are resolved for two tandem HAMP domains on a phototaxis transducer. Conclusion: A molecular mechanism for HAMP domain switching and signal transmission is proposed. Significance: The HAMP switching and relay mechanism is important to many signal transduction proteins.

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Section: Discussionsupporting

confidence: 70%

HAMP Domain Signal Relay Mechanism in a Sensory Rhodopsin-Transducer Complex

Wang

Sasaki

Tsai

et al. 2012

Journal of Biological Chemistry

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“…Similar in vivo studies of Aer, an MCP‐like aerosensor, have also indicated a four‐helix bundle HAMP structure (Watts et al ., 2008). In HtrII, an MCP‐like transducer that interacts with the sensory rhodopsin photoreceptor of Natronomonas pharaonis , HAMP signalling is accompanied by changes in the diffusion coefficients of AS1 and AS2 (Inoue et al ., 2008) and by conversion from a ‘dynamic’ state to a ‘compact’ structure (Doebber et al ., 2008). Both results are at least consistent with a four‐helix bundle.…”

Section: Discussionmentioning

confidence: 99%

Mutational analyses of HAMP helices suggest a dynamic bundle model of input–output signalling in chemoreceptors

Zhou

Ames

Parkinson³

2009

Molecular Microbiology

123

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SummaryTo test the gearbox model of HAMP signalling in the Escherichia coli serine receptor, Tsr, we generated a series of amino acid replacements at each residue of the AS1 and AS2 helices. The residues most critical for Tsr function defined hydrophobic packing faces consistent with a four-helix bundle. Suppression patterns of helix lesions conformed to the predicted packing layers in the bundle. Although the properties and patterns of most AS1 and AS2 lesions were consistent with both proposed gearbox structures, some mutational features specifically indicate the functional importance of an x-da bundle over an alternative a-d bundle. These genetic data suggest that HAMP signalling could simply involve changes in the stability of its x-da bundle. We propose that Tsr HAMP controls output signals by modulating destabilizing phase clashes between the AS2 helices and the adjoining kinase control helices. Our model further proposes that chemoeffectors regulate HAMP bundle stability through a control cable connection between the transmembrane segments and AS1 helices. Attractant stimuli, which cause inward piston displacements in chemoreceptors, should reduce cable tension, thereby stabilizing the HAMP bundle. This study shows how transmembrane signalling and HAMP input-output control could occur without the helix rotations central to the gearbox model.

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“…2 This model is based on FRET, 28 Fourier transform infrared 31 spectroscopy, EPR 26,30 spectroscopy, isothermal titration calorimetry 27 and molecular dynamics simulations. 32 However, a different structural rearrangement was found in the crystal structure of the excited state. 29 After light absorption, the retinal isomerises, and the water cluster next to the retinal binding in the extracellular part of the channel is reorganised.…”

Section: Conformational Answer After Light Activation Varies With Tramentioning

confidence: 98%

Single-Molecule Force Spectroscopy Measures Structural Changes Induced by Light Activation and Transducer Binding in Sensory Rhodopsin II

Oberbarnscheidt

Janissen

Martell

et al. 2009

Journal of Molecular Biology

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Signal Transmission through the HtrII Transducer Alters the Interaction of Two α-Helices in the HAMP Domain

Cited by 13 publications

References 27 publications

HAMP Domain Signal Relay Mechanism in a Sensory Rhodopsin-Transducer Complex

HAMP Domain Signal Relay Mechanism in a Sensory Rhodopsin-Transducer Complex

Mutational analyses of HAMP helices suggest a dynamic bundle model of input–output signalling in chemoreceptors

Single-Molecule Force Spectroscopy Measures Structural Changes Induced by Light Activation and Transducer Binding in Sensory Rhodopsin II

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