Asymmetric activation mechanism of a homodimeric red light-regulated photoreceptor
Organisms adapt to environmental cues using diverse signaling networks. In order to sense and integrate light for regulating various biological functions, photoreceptor proteins have evolved in a modular way. This modularity is targeted in the development of optogenetic tools enabling the control of...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2018-06-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/34815 |
| _version_ | 1811253391852044288 |
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| author | Geoffrey Gourinchas Udo Heintz Andreas Winkler |
| author_facet | Geoffrey Gourinchas Udo Heintz Andreas Winkler |
| author_sort | Geoffrey Gourinchas |
| collection | DOAJ |
| description | Organisms adapt to environmental cues using diverse signaling networks. In order to sense and integrate light for regulating various biological functions, photoreceptor proteins have evolved in a modular way. This modularity is targeted in the development of optogenetic tools enabling the control of cellular events with high spatiotemporal precision. However, the limited understanding of signaling mechanisms impedes the rational design of innovative photoreceptor-effector couples. Here, we reveal molecular details of signal transduction in phytochrome-regulated diguanylyl cyclases. Asymmetric structural changes of the full-length homodimer result in a functional heterodimer featuring two different photoactivation states. Structural changes around the cofactors result in a quasi-translational rearrangement of the distant coiled-coil sensor-effector linker. Eventually, this regulates enzymatic activity by modulating the dimer interface of the output domains. Considering the importance of phytochrome heterodimerization in plant signaling, our mechanistic details of asymmetric photoactivation in a bacterial system reveal novel aspects of the evolutionary adaptation of phytochromes. |
| first_indexed | 2024-04-12T16:50:13Z |
| format | Article |
| id | doaj.art-bd3cd1740be24e5d96421e7d527ac78b |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T16:50:13Z |
| publishDate | 2018-06-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-bd3cd1740be24e5d96421e7d527ac78b2022-12-22T03:24:26ZengeLife Sciences Publications LtdeLife2050-084X2018-06-01710.7554/eLife.34815Asymmetric activation mechanism of a homodimeric red light-regulated photoreceptorGeoffrey Gourinchas0https://orcid.org/0000-0003-2543-3518Udo Heintz1Andreas Winkler2https://orcid.org/0000-0001-6221-9671Institute of Biochemistry, Graz University of Technology, Graz, AustriaMax Planck Institute for Medical Research, Heidelberg, GermanyInstitute of Biochemistry, Graz University of Technology, Graz, AustriaOrganisms adapt to environmental cues using diverse signaling networks. In order to sense and integrate light for regulating various biological functions, photoreceptor proteins have evolved in a modular way. This modularity is targeted in the development of optogenetic tools enabling the control of cellular events with high spatiotemporal precision. However, the limited understanding of signaling mechanisms impedes the rational design of innovative photoreceptor-effector couples. Here, we reveal molecular details of signal transduction in phytochrome-regulated diguanylyl cyclases. Asymmetric structural changes of the full-length homodimer result in a functional heterodimer featuring two different photoactivation states. Structural changes around the cofactors result in a quasi-translational rearrangement of the distant coiled-coil sensor-effector linker. Eventually, this regulates enzymatic activity by modulating the dimer interface of the output domains. Considering the importance of phytochrome heterodimerization in plant signaling, our mechanistic details of asymmetric photoactivation in a bacterial system reveal novel aspects of the evolutionary adaptation of phytochromes.https://elifesciences.org/articles/34815photoreceptorphytochromeGGDEFallosterysensor-effectorsignaling |
| spellingShingle | Geoffrey Gourinchas Udo Heintz Andreas Winkler Asymmetric activation mechanism of a homodimeric red light-regulated photoreceptor eLife photoreceptor phytochrome GGDEF allostery sensor-effector signaling |
| title | Asymmetric activation mechanism of a homodimeric red light-regulated photoreceptor |
| title_full | Asymmetric activation mechanism of a homodimeric red light-regulated photoreceptor |
| title_fullStr | Asymmetric activation mechanism of a homodimeric red light-regulated photoreceptor |
| title_full_unstemmed | Asymmetric activation mechanism of a homodimeric red light-regulated photoreceptor |
| title_short | Asymmetric activation mechanism of a homodimeric red light-regulated photoreceptor |
| title_sort | asymmetric activation mechanism of a homodimeric red light regulated photoreceptor |
| topic | photoreceptor phytochrome GGDEF allostery sensor-effector signaling |
| url | https://elifesciences.org/articles/34815 |
| work_keys_str_mv | AT geoffreygourinchas asymmetricactivationmechanismofahomodimericredlightregulatedphotoreceptor AT udoheintz asymmetricactivationmechanismofahomodimericredlightregulatedphotoreceptor AT andreaswinkler asymmetricactivationmechanismofahomodimericredlightregulatedphotoreceptor |