Seeing the light with BLUF proteins

Park, Sam-Yong; Tame, J.R.H.

doi:10.1007/s12551-017-0258-6

Cited by 48 publications

(55 citation statements)

References 63 publications

(80 reference statements)

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“…Next, we describe how PixD relays its light-dependent signal as an example of the intermolecular interactions between its BLUF domain and its downstream factor, PixE. Signal relays involving other BLUF domains and their downstream factors have been recently summarized (Lindner et al 2015 ; Nudel and Hellingwerf 2015 ; Park and Tame 2017 ).…”

Section: Pixd-dependent Signal-relay Mechanismsmentioning

confidence: 99%

Light-induced chromophore and protein responses and mechanical signal transduction of BLUF proteins

Fujisawa

Masuda

2017

Biophys Rev

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Photoreceptor proteins have been used to study how protein conformational changes are induced by alterations in their environments and how their signals are transmitted to downstream factors to dictate physiological responses. These proteins are attractive models because their signal transduction aspects and structural changes can be precisely regulated in vivo and in vitro based on light intensity. Among the known photoreceptors, members of the blue light–using flavin (BLUF) protein family have been well characterized with regard to how they control various light-dependent physiological responses in several microorganisms. Herein, we summarize our current understanding of their photoactivation and signal-transduction mechanisms. For signal transduction, we review recent studies concerning how the BLUF protein, PixD, transmits a light-induced signal to its downstream factor, PixE, to modulate phototaxis of the cyanobacterium Synechocystis sp. PCC6803.

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Section: Pixd-dependent Signal-relay Mechanismsmentioning

confidence: 99%

Light-induced chromophore and protein responses and mechanical signal transduction of BLUF proteins

Fujisawa

Masuda

2017

Biophys Rev

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“…BLUF (Blue Light Using Flavin) domains are light-triggered switches that control enzyme activity or gene expression in response to blue light 1 . These photosensors bind riboflavin (RB) derivatives as chromophores, namely FMN (Flavin Mononucleotide) or FAD (Flavin Adenine Dinucleotide) 2 .…”

Section: Introductionmentioning

confidence: 99%

“…These photosensors bind riboflavin (RB) derivatives as chromophores, namely FMN (Flavin Mononucleotide) or FAD (Flavin Adenine Dinucleotide) 2 . Many BLUF proteins, including AppA and PAC, carry an extra domain adjacent to the BLUF domain, with enzymatic activity or other properties 1 . However, the majority of bacterial BLUF proteins, do not possess an effector domain covalently linked 2 , and consist solely of the BLUF core and a C-terminal extension 1 .…”

Section: Introductionmentioning

confidence: 99%

BlsA integrates light and temperature signals into iron metabolism through Fur in the human pathogen Acinetobacter baumannii

Tuttobene

Cribb

Mussi

2018

Sci Rep

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Light modulates global features of the important human pathogen Acinetobacter baumannii lifestyle including metabolism, tolerance to antibiotics and virulence, most of which depend on the short BLUF-type photoreceptor BlsA. In this work, we show that the ability to circumvent iron deficiency is also modulated by light at moderate temperatures, and disclose the mechanism of signal transduction by showing that BlsA antagonizes the functioning of the ferric uptake regulator (Fur) in a temperature-dependent manner. In fact, we show that BlsA interacts with Fur in the dark at 23 °C, while the interaction is significantly weakened under blue light. Moreover, under iron deprived conditions, expression of Fur-regulated Acinetobactin siderophore genes is only induced in the dark in a BlsA-dependent manner. Finally, growth under iron deficiency is supported in the dark rather than under blue light at moderate temperatures through BlsA. The data is consistent with a model in which BlsA might sequester the repressor from the corresponding operator-promoters, allowing Acinetobactin gene expression. The photoregulation of iron metabolism is lost at higher temperatures such as 30 °C, consistent with fading of the BlsA-Fur interaction at this condition. Overall, we provide new understanding on the functioning of the widespread Fur regulator as well as short-BLUFs.

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“…Photoactivation of group I BLUF proteins controls enzymatic activity (e.g., adenylate cyclase), whereas group II proteins display differences in their oligomeric state. Although the mechanism of light‐transmitted structural changes for the LOV domain is relatively well defined, the corresponding mechanism for the BLUF domain is controversial and may very well differ among different BLUF‐containing proteins …”

Section: Light‐capturing Antennas Of Photoresponsive Proteinsmentioning

confidence: 99%

“…Although the mechanism of lighttransmitted structural changes fort he LOV domain is relatively well defined, the corresponding mechanism for the BLUF domain is controversial and may very welld iffer among different BLUF-containing proteins. [30] Cryptochromes (Crys) are FAD/pterin-binding photoreceptors approximately % 500 residues in length. [31] They are present in plants and animals and exhibit ap ronounceds tructural homology to the family of DNA repair enzymes knowna sp hotolyases.…”

Section: Flavin-dependent Photoreceptorsmentioning

confidence: 99%

Optogenetics: A Primer for Chemists

O’Banion

Lawrence

2018

ChemBioChem

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The field of optogenetics uses genetically encoded, lightresponsive proteins to control physiological processes. This technology has been hailed as the one of the ten big ideas in brain science in the past decade, the breakthrough of the decade, and the method of the year in 2010 and again in 2014. The excitement evidenced by these proclamations is confirmed by a couple of impressive numbers. The term "optogenetics" was coined in 2006. As of December 2017, "optogenetics" is found in the title or abstract of almost 1600 currently funded National Institutes of Health grants. In addition, nearly 600 reviews on optogenetics have appeared since 2006, which averages out to approximately one review per week! However, in spite of these impressive numbers, the potential applications and implications of optogenetics are not even close to being fully realized. This is due, in large part, to the challenges associated with the design of optogenetic analogues of endogenous proteins. This review is written from a chemist's perspective, with a focus on the molecular strategies that have been developed for the construction of optogenetic proteins.

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Seeing the light with BLUF proteins

Cited by 48 publications

References 63 publications

Light-induced chromophore and protein responses and mechanical signal transduction of BLUF proteins

Light-induced chromophore and protein responses and mechanical signal transduction of BLUF proteins

BlsA integrates light and temperature signals into iron metabolism through Fur in the human pathogen Acinetobacter baumannii

Optogenetics: A Primer for Chemists

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