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Transducer binding establishes localized interactions to tune sensory rhodopsin II
Biotechnology Center, University of Technology, Dresden, Germany.ORCID iD: 0000-0001-9919-0075
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2008 (English)In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 16, no 8, p. 1206-1213Article in journal (Refereed) Published
Abstract [en]

In haloarchaea, sensory rhodopsin II (SRII) mediates a photophobic response to avoid photo-oxidative damage in bright light. Upon light activation the receptor undergoes a conformational change that activates a tightly bound transducer molecule (HtrII), which in turn by a chain of homologous reactions transmits the signal to the chemotactic eubacterial two-component system. Here, using single-molecule force spectroscopy, we localize and quantify changes to the intramolecular interactions within SRII of Natronomonas pharaonis (NpSRII) upon NpHtrII binding. Transducer binding affected the interactions at transmembrane alpha helices F and G of NpSRII to which the transducer was in contact. Remarkably, the interactions were distributed asymmetrically and significantly stabilized alpha helix G entirely but alpha helix F only at its extracellular tip. These findings provide unique insights into molecular mechanisms that "prime" the complex for signaling, and guide the receptor toward transmitting light-activated structural changes to its cognate transducer.

Place, publisher, year, edition, pages
2008. Vol. 16, no 8, p. 1206-1213
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Structural Biology
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URN: urn:nbn:se:umu:diva-156774DOI: 10.1016/j.str.2008.04.014PubMedID: 18682222OAI: oai:DiVA.org:umu-156774DiVA, id: diva2:1291988
Available from: 2019-02-26 Created: 2019-02-26 Last updated: 2019-03-07Bibliographically approved

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Cisneros, David A.

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