Role of a short light, oxygen, voltage (LOV) domain protein in blue light- and singlet oxygen-dependent gene regulation in Rhodobacter sphaeroides

Metz, Sebastian; Jäger, Andreas; Klug, Gabriele

doi:10.1099/mic.0.054700-0

Cited by 26 publications

(40 citation statements)

References 69 publications

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“…Previous studies of RsLOV from R. sphaeroides 2.4.1 detected the protein in both the cytoplasm and the membrane fractions (39), making a signal to a transporter or a channel protein not unreasonable. RsLOV has been linked to a regulatory role in photosynthetic gene expression, carbohydrate metabolism, chemotaxis, and the response to photooxidative stress (51). RsLOV also impacts blue light-dependent gene expression and redox-dependent regulation.…”

Section: Discussionmentioning

confidence: 99%

“…Upstream of RsLOV is a hypothetical protein of 224 residues ( rsp 2268), and a 409 aa glycogen-1-phosphate adenylyltransferase ( rsp 2266). Previous studies of RsLOV from a similar R. sphaeroides strain implicated the protein in photosynthetic gene expression in a manner similar to that of the other two photoreceptor proteins of R.sphaeroides , AppA and CryB (51). Thus, functional and gene clustering analyses potentially involve RsLOV function in carbohydrate metabolism, chemotaxis, and cellular response to photooxidative stress.…”

Section: Introductionmentioning

confidence: 89%

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Light-Induced Subunit Dissociation by a Light–Oxygen–Voltage Domain Photoreceptor from Rhodobacter sphaeroides

2013

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Light-oxygen-voltage (LOV) domains bind a flavin chromophore to serve as blue light sensors in a wide range of eukaryotic and prokaryotic proteins. LOV domains are associated with a variable effector domain or a separate protein signaling partner to execute a wide variety of functions that include regulation of kinases, generation of antisigma-factor antagonists, and regulation of circadian clocks. Here we present the crystal structure, photocycle kinetics, association properties, and spectroscopic features of a full-length LOV protein from Rhodobacter sphaeroides (RsLOV). RsLOV exhibits N-terminal and C-terminal helical extensions that form an unusual helical bundle at its dimer interface with some resemblance to the helical transducer of sensory rhodopsin II. The blue light-induced conformational changes of RsLOV revealed from a comparison of light and dark state crystal structures support a shared signaling mechanism of LOV domain proteins that originates with the light-induced formation of a flavin-cysteinyl photoadduct. Adduct formation disrupts hydrogen bonding in the active site and propagates structural changes through the LOV domain core to the N- and C-terminal extensions. Single residue variants in the active site and dimer interface of RsLOV alter photoadduct lifetimes and induce structural changes that perturb oligomeric state. Size exclusion chromatography, multi-angle light scattering, small-angle X-ray scattering and cross-linking studies indicate that RsLOV dimerizes in the dark, but upon light excitation, dissociates into monomers. This light-induced switch in oligomeric state may prove useful for engineering molecular associations in controlled cellular settings.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 89%

Light-Induced Subunit Dissociation by a Light–Oxygen–Voltage Domain Photoreceptor from Rhodobacter sphaeroides

2013

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“…Double BL and redox sensing has been extensively described for the BLUF protein AppA from Rhodobacter sphaeroides , a key regulator of photosynthesis gene expression, where nevertheless oxygen is sensed chiefly by a distinct heme‐binding domain . A complex BL/redox–driven regulation of gene expression in R. sphaeroides , possibly also including a LOV protein and a Cry, is aimed to maximize photosynthesis under favorable conditions, and to reduce it when the risk of photo‐oxidative damage is high .…”

Section: Lov Domains and The Redox Question In Fl‐bluesmentioning

confidence: 99%

“…They represent about 18% of listed bacterial LOV proteins . In Rhodobacter sphaeroides , the Rs LOV protein has been demonstrated to act synergetically with the BLUF protein AppA, and to downregulate the expression of genes involved in photosynthesis and in photo‐oxidative stress response, under control of the σ F factor . As mentioned above, Rs AppA is a BLUF protein that integrates BL and redox signaling, through two different sensing domains .…”

Section: Lov‐regulated Patterns and Lifestyles In Bacteriamentioning

confidence: 99%

The Evolution and Functional Role of Flavin‐based Prokaryotic Photoreceptors

Losi

Mandalari

Gärtner

2015

Photochem & Photobiology

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Flavin-based photoreceptor proteins of the LOV (light, oxygen and voltage) superfamily are ubiquitous and appear to be essential blue-light sensing systems not only in plants, algae and fungi, but also in prokaryotes, where they are represented in more than 10% of known species. Despite their broad occurrence, only in few cases LOV proteins have been correlated with important phenomena such as bacterial infectivity, selective growth patterns or/and stress responses; nevertheless these few known roles are helping us understand the multiple ways by which prokaryotes can exploit these soluble blue-light photoreceptors. Given the large number of sequences now deposited in databases, it becomes meaningful to define a signature for bona fide LOV domains, a procedure that facilitates identification of proteins with new properties and phylogenetic analysis. The latter clearly evidences that a class of LOV proteins from alpha-proteobacteria is the closest prokaryotic relative of eukaryotic LOV domains, whereas cyanobacterial sequences cluster with the archaeal and the other bacterial LOV domains. Distance trees built for LOV domains suggest complex evolutionary patterns, possibly involving multiple horizontal gene transfer events. Based on available data, the in vivo relevance and evolution of prokaryotic LOV is discussed.

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“…, proposed unknown regulator. Interestingly, transcriptome profiling suggests that yet another blue light-sensing protein RsLOV (RSP2228) (Hendrischk, Moldt, Frühwirth, & Klug, 2009b;Metz, Jäger, & Klug, 2012b), in the LOV (light-oxygen-voltage) domain family (Losi & Gartner, 2011), may be involved in the RpoE-dependant response to photooxidative stress. (For colour version of this figure, the reader is referred to the online version of this book.)…”

Section: The Ppsr Regulonmentioning

confidence: 99%