Cyanobacteriochromes in full color and three dimensions

Rockwell, Nathan C.; Ohlendorf, Robert; Möglich, Andreas

doi:10.1073/pnas.1220690110

Cited by 29 publications

(34 citation statements)

References 21 publications

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“…12,36,61,102 Similar sequence signatures recur in the linkers between consecutive (photo)sensor modules which argues that coiled coils are also instrumental for the integration of multiple signals. This notion is implied by the tandem arrangements of regularly spaced PAS 15 and GAF domains, for example, in cyanobacteriochromes, 155 evident in many receptors, 56 and it has been borne out experimentally in the engineered SHK YHF. 15 Derived from YF1, YHF combines a LOV with a heme-binding PAS sensor and responds to the signals blue light and molecular oxygen in positive cooperative manner.…”

Section: The Dynamics Of α-Helical Coiled Coilsmentioning

confidence: 99%

Signal transduction in photoreceptor histidine kinases

Möglich

2019

Protein Science

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Two‐component systems (TCS) constitute the predominant means by which prokaryotes read out and adapt to their environment. Canonical TCSs comprise a sensor histidine kinase (SHK), usually a transmembrane receptor, and a response regulator (RR). In signal‐dependent manner, the SHK autophosphorylates and in turn transfers the phosphoryl group to the RR which then elicits downstream responses, often in form of altered gene expression. SHKs also catalyze the hydrolysis of the phospho‐RR, hence, tightly adjusting the overall degree of RR phosphorylation. Photoreceptor histidine kinases are a subset of mostly soluble, cytosolic SHKs that sense light in the near‐ultraviolet to near‐infrared spectral range. Owing to their experimental tractability, photoreceptor histidine kinases serve as paradigms and provide unusually detailed molecular insight into signal detection, decoding, and regulation of SHK activity. The synthesis of recent results on receptors with light‐oxygen‐voltage, bacteriophytochrome and microbial rhodopsin sensor units identifies recurring, joint signaling strategies. Light signals are initially absorbed by the sensor module and converted into subtle rearrangements of α helices, mostly through pivoting and rotation. These conformational transitions propagate through parallel coiled‐coil linkers to the effector unit as changes in left‐handed superhelical winding. Within the effector, subtle conformations are triggered that modulate the solvent accessibility of residues engaged in the kinase and phosphatase activities. Taken together, a consistent view of the entire trajectory from signal detection to regulation of output emerges. The underlying allosteric mechanisms could widely apply to TCS signaling in general.

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Section: The Dynamics Of α-Helical Coiled Coilsmentioning

confidence: 99%

Signal transduction in photoreceptor histidine kinases

Möglich

2019

Protein Science

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“…SL2, 2-fold difference (39); BlrP1, 4-fold difference (40); and the C-terminal fragment of Cph2, 2-fold difference (19)), suggesting that SesA is suitable for the study of light regulation mechanisms and as an optogenetic tool (41). Recently obtained crystal structures of CBCR-GAF domains suggest that they form a helical bundle by dimerization and transduce their signals to their C termini via these helices (6,8). Dimerization of GGDEF domain proteins is necessary for their diguanylate cyclase activities (31,42).…”

Section: ) the Combination Of Ms Ms/ms And Ms/ms/ms Definitively Imentioning

confidence: 99%

Cyanobacteriochrome SesA Is a Diguanylate Cyclase That Induces Cell Aggregation in Thermosynechococcus

Enomoto

Nomura

Shimada

et al. 2014

Journal of Biological Chemistry

102

109

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“…These include Phys that use Pfr as the dark-adapted state (bathy-Phys), thus requiring far-red light for photoactivation, Phys lacking the PAS domain (PASless), and Phys missing the PAS and PHY domains with the GAF domain sometimes arranged in repeated units, each with its own photochromic bilin (1,3,20,21). This diversity is particularly evident in cyanobacteria, where a collection of Phy variants called cyanobacteriochromes are expressed with remarkably diverse end states, including violet/blue, violet/ orange, blue/green, green/red, and red/green light-absorbing pairs (6,22).…”

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Crystallographic and Electron Microscopic Analyses of a Bacterial Phytochrome Reveal Local and Global Rearrangements during Photoconversion

Burgie

Wang

Bussell

et al. 2014

Journal of Biological Chemistry

112

223

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Background: Phytochromes are dimeric bili-proteins central to photoperception by plants and microorganisms. Results: An informative perspective on photoconversion from the dark-adapted to the photoactivated state was provided by crystallographic and electron microscopic analyses of a bacterial version. Conclusion: Light-induced conformational changes in the bilin induce a large scale reorientation of the sister output modules. Significance: The structures offer a model for signal transmission by phytochromes.

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Cyanobacteriochromes in full color and three dimensions

Cited by 29 publications

References 21 publications

Signal transduction in photoreceptor histidine kinases

Signal transduction in photoreceptor histidine kinases

Cyanobacteriochrome SesA Is a Diguanylate Cyclase That Induces Cell Aggregation in Thermosynechococcus

Crystallographic and Electron Microscopic Analyses of a Bacterial Phytochrome Reveal Local and Global Rearrangements during Photoconversion

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