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https://www.readbyqxmd.com/read/29042655/electron-transfer-pathways-in-a-light-oxygen-voltage-lov-protein-devoid-of-the-photoactive-cysteine
#1
Benita Kopka, Kathrin Magerl, Anton Savitsky, Mehdi D Davari, Katrin Röllen, Marco Bocola, Bernhard Dick, Ulrich Schwaneberg, Karl-Erich Jaeger, Ulrich Krauss
Blue-light absorption by the flavin chromophore in light, oxygen, voltage (LOV) photoreceptors triggers photochemical reactions that lead to the formation of a flavin-cysteine adduct. While it has long been assumed that adduct formation is essential for signaling, it was recently shown that LOV photoreceptor variants devoid of the photoactive cysteine can elicit a functional response and that flavin photoreduction to the neutral semiquinone radical is sufficient for signal transduction. Currently, the mechanistic basis of the underlying electron- (eT) and proton-transfer (pT) reactions is not well understood...
October 17, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28893998/engineering-a-light-activated-caspase-3-for-precise-ablation-of-neurons-in-vivo
#2
Ashley D Smart, Roland A Pache, Nathan D Thomsen, Tanja Kortemme, Graeme W Davis, James A Wells
The circuitry of the brain is characterized by cell heterogeneity, sprawling cellular anatomy, and astonishingly complex patterns of connectivity. Determining how complex neural circuits control behavior is a major challenge that is often approached using surgical, chemical, or transgenic approaches to ablate neurons. However, all these approaches suffer from a lack of precise spatial and temporal control. This drawback would be overcome if cellular ablation could be controlled with light. Cells are naturally and cleanly ablated through apoptosis due to the terminal activation of caspases...
September 26, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28754922/shadowy-a-dark-yellow-fluorescent-protein-for-flim-based-fret-measurement
#3
Hideji Murakoshi, Akihiro C E Shibata
Fluorescence lifetime imaging microscopy (FLIM)-based Förster resonance energy transfer (FRET) measurement (FLIM-FRET) is one of the powerful methods for imaging of intracellular protein activities such as protein-protein interactions and conformational changes. Here, using saturation mutagenesis, we developed a dark yellow fluorescent protein named ShadowY that can serve as an acceptor for FLIM-FRET. ShadowY is spectrally similar to the previously reported dark YFP but has a much smaller quantum yield, greater extinction coefficient, and superior folding property...
July 28, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28715126/an-engineered-photoswitchable-mammalian-pyruvate-kinase
#4
EDITORIAL
Stefanie Gehrig, Jamie A Macpherson, Paul C Driscoll, Alastair Symon, Stephen R Martin, James I MacRae, Jens Kleinjung, Franca Fraternali, Dimitrios Anastasiou
Changes in allosteric regulation of glycolytic enzymes have been linked to metabolic reprogramming involved in cancer. Remarkably, allosteric mechanisms control enzyme function at significantly shorter time-scales compared to the long-term effects of metabolic reprogramming on cell proliferation. It remains unclear if and how the speed and reversibility afforded by rapid allosteric control of metabolic enzymes is important for cell proliferation. Tools that allow specific, dynamic modulation of enzymatic activities in mammalian cells would help address this question...
September 2017: FEBS Journal
https://www.readbyqxmd.com/read/28663371/functional-characterization-of-a-constitutively-active-kinase-variant-of-arabidopsis-phototropin-1
#5
COMPARATIVE STUDY
Jan Petersen, Shin-Ichiro Inoue, Sharon M Kelly, Stuart Sullivan, Toshinori Kinoshita, John M Christie
Phototropins (phots) are plasma membrane-associated serine/threonine kinases that coordinate a range of processes linked to optimizing photosynthetic efficiency in plants. These photoreceptors contain two light-, oxygen-, or voltage-sensing (LOV) domains within their N terminus, with each binding one molecule of flavin mononucleotide as a UV/blue light-absorbing chromophore. Although phots contain two LOV domains, light-induced activation of the C-terminal kinase domain and subsequent receptor autophosphorylation is controlled primarily by the A'α-LOV2-Jα photosensory module...
August 18, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28530801/hydrogen-bonding-environment-of-the-n3-h-group-of-flavin-mononucleotide-in-the-light-oxygen-voltage-domains-of-phototropins
#6
Tatsuya Iwata, Dai Nozaki, Atsushi Yamamoto, Takayuki Koyama, Yasuzo Nishina, Kiyoshi Shiga, Satoru Tokutomi, Masashi Unno, Hideki Kandori
The light oxygen voltage (LOV) domain is a flavin-binding blue-light receptor domain, originally found in a plant photoreceptor phototropin (phot). Recently, LOV domains have been used in optogenetics as the photosensory domain of fusion proteins. Therefore, it is important to understand how LOV domains exhibit light-induced structural changes for the kinase domain regulation, which enables the design of LOV-containing optogenetics tools with higher photoactivation efficiency. In this study, the hydrogen bonding environment of the N3-H group of flavin mononucleotide (FMN) of the LOV2 domain from Adiantum neochrome (neo) 1 was investigated by low-temperature Fourier transform infrared spectroscopy...
June 20, 2017: Biochemistry
https://www.readbyqxmd.com/read/28387114/light-induced-conformational-changes-of-lov2-kinase-and-the-linker-region-in-arabidopsis-phototropin2
#7
Akira Takakado, Yusuke Nakasone, Koji Okajima, Satoru Tokutomi, Masahide Terazima
Phototropins (phots) are blue light sensors found in a variety of higher plants and algae. The photochemical reactions of this family of proteins have attracted much attention since their discovery. Phots have two light sensor domains called light-oxygen-voltage 1 (LOV1) and LOV2. After the formation of the characteristic adduct of the LOV domain, a conformational change of the C-terminal region of the LOV2 domain occurs, and characterizing this change is important for understanding biological function, that is, kinase activation...
May 4, 2017: Journal of Physical Chemistry. B
https://www.readbyqxmd.com/read/28293893/yeast-based-screening-system-for-the-selection-of-functional-light-driven-k-channels
#8
Cristian Cosentino, Laura Alberio, Gerhard Thiel, Anna Moroni
Ion channels control the electrical properties of cells by opening and closing (gating) in response to a wide palette of environmental and physiological stimuli. Endowing ion channels with the possibility to be gated by remotely applied stimuli, such as light, provides a tool for in vivo control of cellular functions in behaving animals. We have engineered a synthetic light-gated potassium (K(+)) channel by connecting an exogenous plant photoreceptor LOV2 domain to the K(+) channel pore Kcv. Here, we describe the experimental strategy that we have used to evolve the properties of the channel toward full control of light on pore gating...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28193860/investigations-of-human-myosin-vi-targeting-using-optogenetically-controlled-cargo-loading
#9
Alexander R French, Tobin R Sosnick, Ronald S Rock
Myosins play countless critical roles in the cell, each requiring it to be activated at a specific location and time. To control myosin VI with this specificity, we created an optogenetic tool for activating myosin VI by fusing the light-sensitive Avena sativa phototropin1 LOV2 domain to a peptide from Dab2 (LOVDab), a myosin VI cargo protein. Our approach harnesses the native targeting and activation mechanism of myosin VI, allowing direct inferences on myosin VI function. LOVDab robustly recruits human full-length myosin VI to various organelles in vivo and hinders peroxisome motion in a light-controllable manner...
February 28, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28068090/femtosecond-to-millisecond-dynamics-of-light-induced-allostery-in-the-avena-sativa-lov-domain
#10
Agnieszka A Gil, Sergey P Laptenok, Jarrod B French, James N Iuliano, Andras Lukacs, Christopher R Hall, Igor V Sazanovich, Gregory M Greetham, Adelbert Bacher, Boris Illarionov, Markus Fischer, Peter J Tonge, Stephen R Meech
The rational engineering of photosensor proteins underpins the field of optogenetics, in which light is used for spatiotemporal control of cell signaling. Optogenetic elements function by converting electronic excitation of an embedded chromophore into structural changes on the microseconds to seconds time scale, which then modulate the activity of output domains responsible for biological signaling. Using time-resolved vibrational spectroscopy coupled with isotope labeling, we have mapped the structural evolution of the LOV2 domain of the flavin binding phototropin Avena sativa (AsLOV2) over 10 decades of time, reporting structural dynamics between 100 fs and 1 ms after optical excitation...
February 9, 2017: Journal of Physical Chemistry. B
https://www.readbyqxmd.com/read/27906450/lovtrap-a-versatile-method-to-control-protein-function-with-light
#11
Hui Wang, Klaus M Hahn
We describe a detailed procedure for the use of LOVTRAP, an approach to reversibly sequester and release proteins from cellular membranes using light. In the application described here, proteins that act at the plasma membrane are held at mitochondria in the dark, and reversibly released by irradiation. The technique relies on binding of an engineered Zdk domain to a LOV2 domain, with affinity <30 nM in the dark and >500 nM upon irradiation between 400 and 500 nm. LOVTRAP can be applied to diverse proteins, as it requires attaching only one member of the Zdk/LOV2 pair to the target protein, and the other to the membrane where the target protein is to be sequestered...
December 1, 2016: Current Protocols in Cell Biology
https://www.readbyqxmd.com/read/27766868/photoadduct-formation-from-the-fmn-singlet-excited-state-in-the-lov2-domain-of-chlamydomonas-reinhardtii-phototropin
#12
Jingyi Zhu, Tilo Mathes, Yusaku Hontani, Maxime T A Alexandre, Kee Chua Toh, Peter Hegemann, John T M Kennis
The two Light, Oxygen, and Voltage domains of phototropin are blue-light photoreceptor domains which control various functions in plants and green algae. The key step of the light-driven reaction is the formation of a photoadduct between its FMN chromophore and a conserved cysteine, where the canonical reaction proceeds through the FMN triplet state. Here, complete photoreaction mapping of CrLOV2 from Chlamydomonas reinhardtii phototropin and AsLOV2 from Avena sativa phototropin-1 was realized by ultrafast broadband spectroscopy from femtoseconds to microseconds...
October 21, 2016: Journal of Physical Chemistry Letters
https://www.readbyqxmd.com/read/27714620/lov2-controlled-photoactivation-of-protein-trans-splicing
#13
Anam Qudrat, Abdullah Mosabbir, Kevin Truong
Protein trans-splicing is a posttranslational modification that joins two protein fragments together via a peptide a bond in a process that does not require exogenous cofactors. Towards achieving cellular control, synthetically engineered systems have used a variety of stimuli such as small molecules and light. Recently, split inteins have been engineered to be photoactive by the LOV2 domain (named LOVInC). Herein, we discuss (1) designing of LOV2-activated target proteins (e.g., inteins), (2) selecting feasible splice sites for the extein, and (3) imaging cells that express LOVInC-based target exteins...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/27586333/engineering-and-application-of-lov2-based-photoswitches
#14
S P Zimmerman, B Kuhlman, H Yumerefendi
Cellular optogenetic switches, a novel class of biological tools, have improved our understanding of biological phenomena that were previously intractable. While the design and engineering of these proteins has historically varied, they are all based on borrowed elements from plant and bacterial photoreceptors. In general terms, each of the optogenetic switches designed to date exploits the endogenous light-induced change in photoreceptor conformation while repurposing its effect to target a different biological phenomenon...
2016: Methods in Enzymology
https://www.readbyqxmd.com/read/27537211/unfolding-of-the-c-terminal-j%C3%AE-helix-in-the-lov2-photoreceptor-domain-observed-by-time-resolved-vibrational-spectroscopy
#15
Patrick E Konold, Tilo Mathes, Jörn Weiβenborn, Marie Louise Groot, Peter Hegemann, John T M Kennis
Light-triggered reactions of biological photoreceptors have gained immense attention for their role as molecular switches in their native organisms and for optogenetic application. The light, oxygen, and voltage 2 (LOV2) sensing domain of plant phototropin binds a C-terminal Jα helix that is docked on a β-sheet and unfolds upon light absorption by the flavin mononucleotide (FMN) chromophore. In this work, the signal transduction pathway of LOV2 from Avena sativa was investigated using time-resolved infrared spectroscopy from picoseconds to microseconds...
September 1, 2016: Journal of Physical Chemistry Letters
https://www.readbyqxmd.com/read/27484797/blue-light-excited-light-oxygen-voltage-sensing-domain-2-lov2-triggers-a-rearrangement-of-the-kinase-domain-to-induce-phosphorylation-activity-in-arabidopsis-phototropin1
#16
Mao Oide, Koji Okajima, Sachiko Kashojiya, Yuki Takayama, Tomotaka Oroguchi, Takaaki Hikima, Masaki Yamamoto, Masayoshi Nakasako
Phototropin1 is a blue light (BL) receptor in plants and shows BL-dependent kinase activation. The BL-excited light-oxygen-voltage-sensing domain 2 (LOV2) is primarily responsible for the activation of the kinase domain; however, the molecular mechanism by which conformational changes in LOV2 are transmitted to the kinase domain remains unclear. Here, we investigated BL-induced structural changes of a minimum functional fragment of Arabidopsis phototropin1 composed of LOV2, the kinase domain, and a linker connecting the two domains using small-angle x-ray scattering (SAXS)...
September 16, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27089030/light-induced-nuclear-export-reveals-rapid-dynamics-of-epigenetic-modifications
#17
Hayretin Yumerefendi, Andrew Michael Lerner, Seth Parker Zimmerman, Klaus Hahn, James E Bear, Brian D Strahl, Brian Kuhlman
We engineered a photoactivatable system for rapidly and reversibly exporting proteins from the nucleus by embedding a nuclear export signal in the LOV2 domain from phototropin 1. Fusing the chromatin modifier Bre1 to the photoswitch, we achieved light-dependent control of histone H2B monoubiquitylation in yeast, revealing fast turnover of the ubiquitin mark. Moreover, this inducible system allowed us to dynamically monitor the status of epigenetic modifications dependent on H2B ubiquitylation.
June 2016: Nature Chemical Biology
https://www.readbyqxmd.com/read/26965116/controlling-protein-activity-and-degradation-using-blue-light
#18
Anne P Lutz, Christian Renicke, Christof Taxis
Regulation of protein stability is a fundamental process in eukaryotic cells and pivotal to, e.g., cell cycle progression, faithful chromosome segregation, or protein quality control. Synthetic regulation of protein stability requires conditional degradation sequences (degrons) that induce a stability switch upon a specific signal. Fusion to a selected target protein permits to influence virtually every process in a cell. Light as signal is advantageous due to its precise applicability in time, space, quality, and quantity...
2016: Methods in Molecular Biology
https://www.readbyqxmd.com/read/26940144/post-translational-control-of-protein-function-with-light-using-a-lov-intein-fusion-protein
#19
D C Jones, I N Mistry, A Tavassoli
Methods for the post-translational control of protein function with light hold much value as tools in cell biology. To this end, we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa. The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light in bacterial and human cells.
April 2016: Molecular BioSystems
https://www.readbyqxmd.com/read/26815763/molecular-mechanism-of-phototropin-light-signaling
#20
REVIEW
Koji Okajima
Phototropin (phot) is a blue light (BL) receptor kinase involved in the BL responses of several species, ranging from green algae to higher plants. Phot converts BL signals from the environment into biochemical signals that trigger cellular responses. In phot, the LOV1 and LOV2 domains of the N-terminal region utilize BL for cyclic photoreactions and regulate C-terminal serine/threonine kinase (STK) activity. LOV2-STK peptides are the smallest functional unit of phot and are useful for understanding regulation mechanisms...
March 2016: Journal of Plant Research
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