Molecular Mechanism of Active Photoprotein Complex Formation
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Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents
International Journal of Molecular Sciences Article Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents 1, 2,3, 1 2, Elena V. Eremeeva y , Tianyu Jiang y , Natalia P. Malikova , Minyong Li * and Eugene S. Vysotski 1,* 1 Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk 660036, Russia; [email protected] (E.V.E.); [email protected] (N.P.M.) 2 Key Laboratory of Chemical Biology (MOE), Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan 250012, China; [email protected] 3 State Key Laboratory of Microbial Technology, Shandong University–Helmholtz Institute of Biotechnology, Shandong University, Qingdao 266237, China * Correspondence: [email protected] (M.L.); [email protected] (E.S.V.); Tel.: +86-531-8838-2076 (M.L.); +7-(391)-249-44-30 (E.S.V.); Fax: +86-531-8838-2076 (M.L.); +7-(391)-290-54-90 (E.S.V.) These authors contributed equally to this work. y Received: 23 June 2020; Accepted: 27 July 2020; Published: 30 July 2020 Abstract: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. -
Bioluminescence Is Produced by a Firefly-Like Luciferase but an Entirely
www.nature.com/scientificreports OPEN New Zealand glowworm (Arachnocampa luminosa) bioluminescence is produced by a Received: 8 November 2017 Accepted: 1 February 2018 frefy-like luciferase but an entirely Published: xx xx xxxx new luciferin Oliver C. Watkins1,2, Miriam L. Sharpe 1, Nigel B. Perry 2 & Kurt L. Krause 1 The New Zealand glowworm, Arachnocampa luminosa, is well-known for displays of blue-green bioluminescence, but details of its bioluminescent chemistry have been elusive. The glowworm is evolutionarily distant from other bioluminescent creatures studied in detail, including the frefy. We have isolated and characterised the molecular components of the glowworm luciferase-luciferin system using chromatography, mass spectrometry and 1H NMR spectroscopy. The purifed luciferase enzyme is in the same protein family as frefy luciferase (31% sequence identity). However, the luciferin substrate of this enzyme is produced from xanthurenic acid and tyrosine, and is entirely diferent to that of the frefy and known luciferins of other glowing creatures. A candidate luciferin structure is proposed, which needs to be confrmed by chemical synthesis and bioluminescence assays. These fndings show that luciferases can evolve independently from the same family of enzymes to produce light using structurally diferent luciferins. Glowworms are found in New Zealand and Australia, and are a major tourist attraction at sites located across both countries. In contrast to luminescent beetles such as the frefy (Coleoptera), whose bioluminescence has been well characterised (reviewed by ref.1), the molecular details of glowworm bioluminescence have remained elusive. Tese glowworms are the larvae of fungus gnats of the genus Arachnocampa, with eight species endemic to Australia and a single species found only in New Zealand2. -
Color-Tunable Bioluminescence Imaging Portfolio for Cell
www.nature.com/scientificreports OPEN Color‑tunable bioluminescence imaging portfolio for cell imaging Shota Tamaki1,3, Nobuo Kitada1,3, Masahiro Kiyama1, Rika Fujii2, Takashi Hirano1, Sung Bae Kim2* & Shojiro Maki1* The present study describes a color‑tunable imaging portfolio together with twelve novel coelenterazine (CTZ) analogues. The three groups of CTZ analogues create diverse hues of bioluminescence (BL) ranging from blue to far red with marine luciferases. We found that the hue completes the whole color palette in the visible region and shows red‑shifted BL with a marine luciferase: for example, Renilla luciferase 8 (RLuc8) and Artifcial Luciferase 16 (ALuc16) show 187 nm‑ and 105 nm‑redshifted spectra, respectively, by simply replacing the substrate CTZ with 1d. The optical properties of the new CTZ analogues were investigated such as the kinetic parameters, dose dependency, and luciferase specifcity. The 2‑series CTZ analogues interestingly have specifcity to ALucs and are completely dark with RLuc derivatives, and 3d is highly specifc to only NanoLuc. We further determined the theoretical background of the red‑shifted BL maximum wavelengths (λBL) values according to the extended π conjugation of the CTZ backbone using Density Functional Theory (DFT) calculations. This color‑tunable BL imaging system provides a useful multicolor imaging portfolio that efciently images molecular events in mammalian cells. Cells provoke diverse intracellular signal transductions in response to a myriad of stimuli from the surround- ing environment1. As cellular systems are such dynamical entities, multiplex imaging is a plausible modality for spying and visualizing such molecular events in cells. To date, bioluminescence (BL) has been broadly utilized for imaging diverse molecular events in the complex context of living subjects2. -
(12) United States Patent (10) Patent No.: US 9,574.223 B2 Cali Et Al
USO095.74223B2 (12) United States Patent (10) Patent No.: US 9,574.223 B2 Cali et al. (45) Date of Patent: *Feb. 21, 2017 (54) LUMINESCENCE-BASED METHODS AND 4,826,989 A 5/1989 Batz et al. PROBES FOR MEASURING CYTOCHROME 4,853,371 A 8/1989 Coy et al. 4,992,531 A 2f1991 Patroni et al. P450 ACTIVITY 5,035,999 A 7/1991 Geiger et al. 5,098,828 A 3/1992 Geiger et al. (71) Applicant: PROMEGA CORPORATION, 5,114,704 A 5/1992 Spanier et al. Madison, WI (US) 5,283,179 A 2, 1994 Wood 5,283,180 A 2f1994 Zomer et al. 5,290,684 A 3/1994 Kelly (72) Inventors: James J. Cali, Verona, WI (US); Dieter 5,374,534 A 12/1994 Zomer et al. Klaubert, Arroyo Grande, CA (US); 5,498.523 A 3, 1996 Tabor et al. William Daily, Santa Maria, CA (US); 5,641,641 A 6, 1997 Wood Samuel Kin Sang Ho, New Bedford, 5,650,135 A 7/1997 Contag et al. MA (US); Susan Frackman, Madison, 5,650,289 A T/1997 Wood 5,726,041 A 3/1998 Chrespi et al. WI (US); Erika Hawkins, Madison, WI 5,744,320 A 4/1998 Sherf et al. (US); Keith V. Wood, Mt. Horeb, WI 5,756.303 A 5/1998 Sato et al. (US) 5,780.287 A 7/1998 Kraus et al. 5,814,471 A 9, 1998 Wood (73) Assignee: PROMEGA CORPORATION, 5,876,946 A 3, 1999 Burbaum et al. 5,976,825 A 11/1999 Hochman Madison, WI (US) 6,143,492 A 11/2000 Makings et al. -
REVIEW Protein-Protein Complexation in Bioluminescence
Protein Cell 2011, 2(12): 957–972 Protein & Cell DOI 10.1007/s13238-011-1118-y REVIEW Protein-protein complexation in bioluminescence ✉ Maxim S. Titushin1, Yingang Feng2, John Lee3, Eugene S. Vysotski4, Zhi-Jie Liu1 1 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China 2 Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China 3 Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA 4 Laboratory of Photobiology, Institute of Biophysics Russian Academy of Sciences, Siberian Branch, Krasnoyarsk 660036, Russia ✉ Correspondence: [email protected] Received October 23, 2011 Accepted November 7, 2011 ABSTRACT INTRODUCTION In this review we summarize the progress made towards Living organisms capable of emitting light have been known understanding the role of protein-protein interactions in to mankind since ancient times (Harvey, 1952; Lee, 2008). the function of various bioluminescence systems of Bioluminescent organisms such as bacteria, fireflies, jellyfish, marine organisms, including bacteria, jellyfish and soft worms, fungi, and fish, are widely dispersed on the corals, with particular focus on methodology used to phylogenetic tree, with a vast majority of species being detect and characterize these interactions. In some marine inhabitants. Believed to emerge “independently” many bioluminescence systems, protein-protein interactions times during evolution, bioluminescence serves vital func- involve an “accessory protein” whereby a stored sub- tions ranging from defense to reproduction, yet in many cases strate is efficiently delivered to the bioluminescent its survival value remains a puzzle (Haddock et al., 2010). enzyme luciferase. Other types of complexation mediate The bioluminescence is an enzymatic reaction, where an energy transfer to an “antenna protein” altering the color enzyme, generically referred to as luciferase, catalyzes and quantum yield of a bioluminescence reaction. -
The Partial Characterization of Select Protist and Tunicate Ca 2+ Activated
Characterizing and defining the optimal conditions for select protist photoprotein activity and testing for photoprotein activity in doliolid tunicates Cheyenne Payne, Scripps Institution of Oceanography, UCSD Mentor: Steven H. Haddock Summer 2016 Keywords: bioluminescence, photoprotein, regeneration, radiolarian, phaeodarian, doliolid ABSTRACT We present the optimal pH, salinity, and Ca2+ concentration necessary for Collozoum photoprotein-activation, as well as the optimal pH for two genera of deep-water phaeodarians. Successful regeneration of radiolarian and phaeodarian photoproteins was achieved. Results on bioluminescence assays with the doliolid tunicate genus, Doliolula, are also presented. INTRODUCTION Bioluminescence and the biochemistry responsible for it have been the subject of research for the past 230 years, since Dubois first discovered the luciferin-luciferase system responsible for bioluminescence in the West Indies Beetle in 1885. The term luciferin refers to an organic compound that releases photons when oxidized, and the luciferase is an enzyme that catalyzes the luciferin’s oxidative light-emitting reaction (Shimomura 2006). For 77 years, the luciferin-luciferase reaction was believed to be the sole source of bioluminescence, until 1962 when the first photoprotein system was described by Shimomura in the jelly Aequorea aequorea (Shimomura et al 1962). Photoproteins are stable protein-compound complexes that emit light when they conformationally change due to a reaction with a cofactor, which is a chemical or molecule that binds to a photoprotein and causes its components to dissociate (Shimomura 2006). Many photoproteins are Ca2+-sensitive, such as those found in coelenterates, and are complexes containing the compound coelenterazine (Shimomura 2006). After a photoprotein has conformationally changed, the protein component is called apo-photoprotein. -
Luciferin Production and Luciferase Transcription in the Bioluminescent Copepod Metridia Lucens
City University of New York (CUNY) CUNY Academic Works Publications and Research Baruch College 2018 Luciferin production and luciferase transcription in the bioluminescent copepod Metridia lucens Michael Tessler American Museum of Natural History Jean P. Gaffney CUNY Bernard M Baruch College Jason M. Crawford Yale University Eric Trautman Yale University Nehaben A. Gujarati CUNY Bernard M Baruch College See next page for additional authors How does access to this work benefit ou?y Let us know! More information about this work at: https://academicworks.cuny.edu/bb_pubs/1104 Discover additional works at: https://academicworks.cuny.edu This work is made publicly available by the City University of New York (CUNY). Contact: [email protected] Authors Michael Tessler, Jean P. Gaffney, Jason M. Crawford, Eric Trautman, Nehaben A. Gujarati, Philip Alatalo, Vincent A. Pierbone, and David F. Gruber This article is available at CUNY Academic Works: https://academicworks.cuny.edu/bb_pubs/1104 Luciferin production and luciferase transcription in the bioluminescent copepod Metridia lucens Michael Tessler1, Jean P. Gaffney2,3, Jason M. Crawford4, Eric Trautman4, Nehaben A. Gujarati2, Philip Alatalo5, Vincent A. Pieribone6 and David F. Gruber2,3 1 Sackler Institute for Comparative Genomics, American Museum of Natural History, New York, NY, USA 2 Department of Natural Sciences, City University of New York, Bernard M. Baruch College, New York, NY, United States of America 3 Biology, City University of New York, Graduate School and University Center, New York, NY, United States of America 4 Department of Chemistry, Yale University, New Haven, CT, United States of America 5 Biology Department, Woods Hole Oceanographic Institution, Woods Hole, MA, United States of America 6 Cellular and Molecular Physiology, Yale University, New Haven, CT, United States of America ABSTRACT Bioluminescent copepods are often the most abundant marine zooplankton and play critical roles in oceanic food webs. -
Redesign of Calcium-Regulated Protein Aequorin Towards the Development
Redesign of calcium-regulated protein aequorin towards the development of a novel ion bioreporter A Thesis submitted to University College London for the degree of Doctor of Philosophy by Evlampia-Kyriaki Dimitriadou Department of Biochemical Engineering University College London UCL April 2014 I, Evlampia-Kyriaki Dimitriadou confirm that the work presented in this thesis is my own. Where information has been derived from other sources, I confirm that this has been indicated in the thesis. - 2 - I dedicate this work to my loving parents, Sophia and Panagiotis - 3 - Abstract This thesis aimed to design novel sensor proteins that can identify and measure various metal ions in vivo and in situ . Metal ions play key role in the metabolism of the cell, and monitoring of calcium has helped interrogate cellular processes such as fertilisation, contraction and apoptosis. Real-time monitoring of more divalent metal ions like zinc and copper is required to gain much needed insight into brain function and associated disorders, such as Alzheimer’s and Parkinson’s disease. Aequorin is a calcium-regulated photoprotein originally isolated from the jellyfish Aequorea victoria . Due to its high sensitivity to calcium and its non-invasive nature, aequorin has been used as a real-time indicator of calcium ions in biological systems for more than forty years. The protein complex consists of the polypeptide chain apoaequorin and a tightly bound chromophore (coelenterazine). Trace amounts of calcium ions trigger conformational changes in the protein, which in turn facilitate the intermolecular oxidation of coelenterazine and concomitant production of CO 2 and a flash of blue light. -
(BRET) for Real Time Detection of Protein-Protein Inte
University of Tennessee, Knoxville Trace: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 5-2008 Application and Optimization of Bioluminescence Resonance Energy Transfer (BRET) for Real Time Detection of Protein-Protein Interactions in Transgenic Arabidopsis as well as Structure-Based Functional Studies on the Active Site of Coelenterazine-dependent Luciferase from Renilla and its Improvement by Protein Engineering Jongchan Woo University of Tennessee - Knoxville Recommended Citation Woo, Jongchan, "Application and Optimization of Bioluminescence Resonance Energy Transfer (BRET) for Real Time Detection of Protein-Protein Interactions in Transgenic Arabidopsis as well as Structure-Based Functional Studies on the Active Site of Coelenterazine-dependent Luciferase from Renilla and its Improvement by Protein Engineering. " PhD diss., University of Tennessee, 2008. https://trace.tennessee.edu/utk_graddiss/355 This Dissertation is brought to you for free and open access by the Graduate School at Trace: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of Trace: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by Jongchan Woo entitled "Application and Optimization of Bioluminescence Resonance Energy Transfer (BRET) for Real Time Detection of Protein-Protein Interactions in Transgenic Arabidopsis as well as Structure-Based Functional Studies on the Active Site of Coelenterazine-dependent Luciferase from Renilla and its Improvement by Protein Engineering." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the requirements for the degree of Doctor of Philosophy, with a major in Plant Sciences. -
Nobel Lecture by Osamu Shimomura
DISCOVERY OF GREEN FLUORESCENT PROTEIN, GFP Nobel Lecture, December 8, 2008 by Osamu Shimomura Marine Biological Laboratory, Woods Hole, MA 02543, USA. PROLOGUE I discovered the green fluorescent protein GFP from the jellyfish Aequorea aequorea in 1961 as a byproduct of the Ca-sensitive photoprotein aequorin (Shimomura et al., 1962; Johnson et al., 1962), and identified its chro- mophore in 1979 (Shimomura, 1979). GFP was a beautiful protein but it remained useless for the next 30 years after the discovery. My story begins in 1945, the year the city of Nagasaki was destroyed by an atomic bomb and World War II ended. At that time I was a 16-year old high school student, and I was working at a factory about 15 km northeast of Nagasaki. I watched the B-29 that carried the atomic bomb heading toward Nagasaki, then soon I was exposed to a blinding bright flash and a strong pressure wave that were caused by a gigantic explosion. I was lucky to sur- vive the war. In the mess after the war, however, I could not find any school to attend. I idled for 2 years, and then I learned that the pharmacy school of Nagasaki Medical College, which had been completely destroyed by the atomic bomb, was going to open a temporary campus near my home. I ap- plied to the pharmacy school and was accepted. Although I didn’t have any interest in pharmacy, it was the only way that I could have some education. After graduating from the pharmacy school, I worked as a teaching assistant at the same school, which was reorganized as a part of Nagasaki University. -
1 the Photoproteins
1 1 The Photoproteins Osamu Shimomura 1.1 Discovery of Photoprotein In 1961, we found an unusual bioluminescent protein in the jellyfi sh Aequorea and named it “aequorin” after its genus name (Shimomura et al. 1962). The protein had the ability to emit light in aqueous solutions merely by the addition of a trace of Ca2+. Surprisingly, it luminesced even in the absence of oxygen. After some studies, we discovered that the light is emitted by an intramolecular reaction that takes place inside the protein molecule, and that the total light emitted is proportional to the amount of protein luminesced. At that time, we simply thought that aequorin was an exceptional protein accidentally made in nature. In 1966, however, we found another unusual bioluminescent protein in the parchment tubeworm Chaetopterus (Shimomura and Johnson 1966). This protein emitted light when a peroxide and a trace of Fe2+ were added in the presence of oxygen, without the participation of any enzyme. The total light emitted was again proportional to the amount of the protein used. These two examples were clearly out of place in the classic concept of the luciferin–luciferase reaction of bioluminescence, wherein luciferin is customarily a relatively heat stable, diffusible organic substrate and luciferase is an enzyme that catalyzes the luminescent oxidation of a luciferin. Considering the possible existence of many similar bioluminescent proteins in luminous organisms, we have introduced the new term “photoprotein” as a convenient, general term to designate unusual bioluminescent proteins such as aequorin and the Chaetopterus bioluminescent protein (Shimomura and Johnson 1966). Thus, “photoprotein” is a general term for the bioluminescent proteins that occur in the light organs of luminous organisms as the major luminescent component and are capable of emitting light in proportion to the amount of protein (Shimomura 1985). -
Coelenterazine-Dependent Luciferases
ISSN 0006-2979, Biochemistry (Moscow), 2015, Vol. 80, No. 6, pp. 714-732. © Pleiades Publishing, Ltd., 2015. Published in Russian in Biokhimiya, 2015, Vol. 80, No. 6, pp. 845-866. REVIEW Coelenterazine-Dependent Luciferases S. V. Markova and E. S. Vysotski* Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, 660036 Krasnoyarsk, Russia; fax: +7 (391) 243-3400; E-mail: [email protected] Received February 25, 2015 Revision received March 4, 2015 Abstract—Bioluminescence is a widespread natural phenomenon. Luminous organisms are found among bacteria, fungi, protozoa, coelenterates, worms, molluscs, insects, and fish. Studies on bioluminescent systems of various organisms have revealed an interesting feature – the mechanisms underlying visible light emission are considerably different in representa- tives of different taxa despite the same final result of this biochemical process. Among the several substrates of biolumines- cent reactions identified in marine luminous organisms, the most commonly used are imidazopyrazinone derivatives such as coelenterazine and Cypridina luciferin. Although the substrate used is the same, bioluminescent proteins that catalyze light emitting reactions in taxonomically remote luminous organisms do not show similarity either in amino acid sequences or in spatial structures. In this review, we consider luciferases of various luminous organisms that use coelenterazine or Cypridina luciferin as a substrate, as well as modifications of these proteins that improve their physicochemical