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Protein-protein complexation in bioluminescence [Text] / M. S. Titushin [et al.] // Protein Cell. - 2011. - Vol. 2, Is. 12. - P957-972, DOI 10.1007/s13238-011-1118-y. - Cited References: 114. - The work was funded by "Fellowship for Young International Scientists" of Chinese Academy of Sciences. This work was supported by the National Natural Science Foundation of China (Grant Nos: 30870483, 31070660, 31021062 and 81072449), Ministry of Science and Technology of China (Nos. 2009DFB30310, 2009CB918803 and 2011CB911103), CAS Research Grants (Nos. YZ200839 and KSCX2-EW-J-3). . - ISSN 1674-800X

РУБ Cell Biology
Рубрики:
GREEN-FLUORESCENT PROTEIN
   LUCIFERIN-BINDING-PROTEIN
   RENILLA-RENIFORMIS LUCIFERASE
   VIBRIO-FISCHERI Y1
   JELLYFISH CLYTIA-GREGARIA
   ALPHA/BETA-HYDROLASE FOLD
   AMINO-ACID-SEQUENCE
   BACTERIAL LUCIFERASE
   ENERGY-TRANSFER
   CRYSTAL-STRUCTURE
Кл.слова (ненормированные):
green-fluorescent protein (GFP) -- photoprotein -- luciferase -- lumazine protein -- Forster resonance energy transfer (FRET) -- docking
Аннотация: In this review we summarize the progress made towards understanding the role of protein-protein interactions in the function of various bioluminescence systems of marine organisms, including bacteria, jellyfish and soft corals, with particular focus on methodology used to detect and characterize these interactions. In some bioluminescence systems, protein-protein interactions involve an "accessory protein" whereby a stored substrate is efficiently delivered to the bioluminescent enzyme luciferase. Other types of complexation mediate energy transfer to an "antenna protein" altering the color and quantum yield of a bioluminescence reaction. Spatial structures of the complexes reveal an important role of electrostatic forces in governing the corresponding weak interactions and define the nature of the interaction surfaces. The most reliable structural model is available for the protein-protein complex of the Ca2+-regulated photoprotein clytin and green-fluorescent protein (GFP) from the jellyfish Clytia gregaria, solved by means of X-ray crystallography, NMR mapping and molecular docking. This provides an example of the potential strategies in studying the transient complexes involved in bioluminescence. It is emphasized that structural studies such as these can provide valuable insight into the detailed mechanism of bioluminescence.

Держатели документа:
[Titushin, Maxim S.
Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[Feng, Yingang] Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Qingdao 266101, Peoples R China
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Lab Photobiol, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Titushin, M.S.; Feng, Y.G.; Lee, J...; Vysotski, E.S.; Liu, Z.J.

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Crystal structure of coelenterazine-binding protein from Renilla muelleri at 1.7 angstrom: Why it is not a calcium-regulated photoprotein [Text] / G. A. Stepanyuk [et al.] // Photochem. Photobiol. Sci. - 2008. - Vol. 7, Is. 4. - P442-447, DOI 10.1039/b716535h. - Cited References: 49 . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
HYDROID OBELIA-GENICULATA
   AMINO-ACID-SEQUENCE
   CA2+-REGULATED PHOTOPROTEINS
   RENIFORMIS LUCIFERASE
   ENERGY-TRANSFER
   CDNA CLONING
   BIOLUMINESCENCE
   AEQUORIN
   PURIFICATION
   EXPRESSION
Аннотация: Bioluminescence in the sea pansy Renilla involves two distinct proteins, a Ca2+-triggered coelenterazine-binding protein (CBP), and Renilla luciferase. CBP contains one tightly bound coelenterazine molecule, which becomes available for reaction with luciferase and O-2 only subsequent to Ca2+ binding. CBP belongs to the EF-hand superfamily of Ca2+-binding proteins and contains three "EF-hand" Ca2+-binding sites. The overall spatial structure of recombinant selenomethionine-labeled CBP determined at 1.7 angstrom, is found to approximate the protein scaffold characteristic of the class of Ca2+-regulated photoproteins. Photoproteins however, catalyze molecular oxygen addition to coelenterazine producing a 2-hydroperoxycoelenterazine intermediate, which is stabilized within the binding cavity in the absence of Ca2+. Addition of Ca2+ triggers the bioluminescence reaction. However in CBP this first step of oxygen addition is not allowed. The different amino acid environments and hydrogen bond interactions within the binding cavity are proposed to account for the different properties of the two classes of proteins.

Держатели документа:
[Liu, Zhi-Jie] Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
[Stepanyuk, Galina A.
Lee, John
Vysotski, Eugene S.
Wang, Bi-Cheng] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Stepanyuk, Galina A.
Markova, Svetlana S.
Frank, Ludmila A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stepanyuk, G.A.; Liu, Z.J.; Markova, S.S.; Frank, L.A.; Lee, J...; Vysotski, E.S.; Wang, B.C.

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Obelin from the bioluminescent marine hydroid Obelia geniculata: Cloning, expression, and comparison of some properties with those of other Ca2+-regulated photoproteins [Text] / S. V. Markova [et al.] // Biochemistry. - 2002. - Vol. 41, Is. 7. - P2227-2236, DOI 10.1021/bi0117910. - Cited References: 54 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
AMINO-ACID-SEQUENCE
   CALCIUM-ACTIVATED PHOTOPROTEINS
   CTENOPHORES MNEMIOPSIS SP
   CA-2+-ACTIVATED PHOTOPROTEIN
   LUMINESCENT PROTEIN
   BINDING-PROTEIN
   BEROE-OVATA
   AEQUORIN
   CDNA
   PURIFICATION
Аннотация: A cDNA encoding the Ca2+-regulated photoprotein of the bioluminescent marine hydroid Obelia geniculata was cloned and sequenced. The cDNA is a 774 bp fragment containing two overlapping open reading frames, one of which contained 585 bp encoding a 195 amino acid polypeptide which obviously has the primary structure of the apoprotein of a calcium-regulated photoprotein. Many of the residues are identical to those in other Ca2+-regulated photoproteins: 86% compared with that from Obelia longissima, 76% with that from Clytia (Phialidium), 64% with that from Aequorea, and 64% with that from Mitrocoma (Halistaura). The obelin from O. geniculata was overexpressed in Escherichia coli, refolded from inclusion bodies, and purified. The yield of highly purified recombinant protein was 55-80 mg/L of LB medium. O. geniculata obelin has absorption maxima at 280 and 460 nm and a shoulder at approximately 310 nm. The calcium-discharged protein loses visible absorption but exhibits a new absorption maximum at 343 nm. The bioluminescence of the obelin from O. geniculata is blue (lambda(max) = 495 nm). In contrast, the fluorescence of the calcium-discharged protein is yellow-green (lambda(max) = 520 nm; excitation at 340 nm). This is in sharp contrast to aequorin in which the bioluminescence and fluorescence emission spectra of the calcium-discharged protein are almost identical (lambda(max) = 465 nm). The Ca2+ concentration-effect curve for O. geniculata obelin is similar to those of many other photoproteins: at [Ca2+] below approximately 10(-8) M, calcium-independent luminescence is observed, and at [Ca2+] approximately 10(-3) M, the luminescence reaches a maximum. Between these extremes, the curve spans a vertical range of almost 8 log units with a maximum slope on a log-log plot of about 2.5. In the absence of Mg2+ the rate constant for the rise of bioluminescence determined by the stopped-flow technique is about 450 s(-1). The effects of Mg2+ on the kinetics of bioluminescence are complicated, but at all concentrations studied they are relatively small compared to the corresponding effects on aequorin luminescence. At least with respect to speed and sensitivity to Mg2+, the obelins from both O. longissima and O. geniculata would appear to be more suitable than aequorin for use as intracellular Ca2+ indicators.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
Univ Washington, Friday Harbor Labs, Friday Harbor, WA 98250 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Vysotski, E.S.; Blinks, J.R.; Burakova, L.P.; Wang, B.C.; Lee, J...

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Purification and ligand exchange protocols for antenna proteins from bioluminescent bacteria [Text] / V. N. Petrushkov [et al.] // Methods Enzymol. - 2000. - Vol. 305. - P. 164-180. - Cited References: 18 . - ISSN 0076-6879

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology
Рубрики:
YELLOW FLUORESCENT PROTEIN
   FISCHERI STRAIN Y-1
   AMINO-ACID-SEQUENCE
   VIBRIO-FISCHERI
   PHOTOBACTERIUM-LEIOGNATHI
   RIBOFLAVIN PROTEIN
   LUMINOUS BACTERIUM
   LUMAZINE PROTEIN
   FMN
   Y1

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Agr Univ Wageningen, Dept Biochem, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petrushkov, V.N.; Gibson, B.G.; Visser, AJWG; Lee, J...

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