메뉴 건너뛰기




Volumn 4, Issue 1, 2008, Pages

Mutational optimization of the coelenterazine-dependent luciferase from Renilla

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ESCHERICHIA COLI; RENILLA; RENILLA LUCIFERASE;

EID: 53749084410     PISSN: None     EISSN: 17464811     Source Type: Journal    
DOI: 10.1186/1746-4811-4-23     Document Type: Article
Times cited : (41)

References (25)
  • 1
    • 0025855388 scopus 로고
    • Isolation and expression of a cDNA encoding Renilla reniformis luciferase
    • 1674607. 10.1073/pnas.88.10.4438
    • Isolation and expression of a cDNA encoding Renilla reniformis luciferase. WW Lorenz RO McCann M Longiaru MJ Cormier, Proc Natl Acad Sci USA 1991 88 4438 4442 1674607 10.1073/pnas.88.10.4438
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4438-4442
    • Lorenz, W.W.1    McCann, R.O.2    Longiaru, M.3    Cormier, M.J.4
  • 2
    • 0037397074 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions using split synthetic Renilla luciferase protein-fragment-assisted complementation
    • 10.1021/ac020731c. 12705589
    • Monitoring protein-protein interactions using split synthetic Renilla luciferase protein-fragment-assisted complementation. R Paulmurugan SS Gambhir, Anal Chem 2003 75 1584 1589 10.1021/ac020731c 12705589
    • (2003) Anal Chem , vol.75 , pp. 1584-1589
    • Paulmurugan, R.1    Gambhir, S.S.2
  • 3
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • 9874787. 10.1073/pnas.96.1.151
    • A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Y Xu DW Piston CH Johnson, Proc Natl Acad Sci USA 1999 96 151 156 9874787 10.1073/pnas.96.1.151
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 4
    • 0015818266 scopus 로고
    • Identification of the product excited states during the chemiluminescent and bioluminescent oxidation of Renilla (sea pansy) luciferin and certain of its analogs
    • 10.1021/bi00746a025. 4147978
    • Identification of the product excited states during the chemiluminescent and bioluminescent oxidation of Renilla (sea pansy) luciferin and certain of its analogs. K Hori JE Wampler JC Matthews MJ Cormier, Biochemistry 1973 12 4463 4468 10.1021/bi00746a025 4147978
    • (1973) Biochemistry , vol.12 , pp. 4463-4468
    • Hori, K.1    Wampler, J.E.2    Matthews, J.C.3    Cormier, M.J.4
  • 5
    • 0017582130 scopus 로고
    • Purification and properties of Renilla reniformis luciferase
    • 10.1021/bi00620a014. 12797
    • Purification and properties of Renilla reniformis luciferase. JC Matthews K Hori MJ Cormier, Biochemistry 1977 16 85 91 10.1021/bi00620a014 12797
    • (1977) Biochemistry , vol.16 , pp. 85-91
    • Matthews, J.C.1    Hori, K.2    Cormier, M.J.3
  • 6
    • 0017761354 scopus 로고
    • Substrate and substrate analogue binding properties of Renilla luciferase
    • 10.1021/bi00643a009. 21679
    • Substrate and substrate analogue binding properties of Renilla luciferase. JC Matthews K Hori MJ Cormier, Biochemistry 1977 16 5217 5220 10.1021/bi00643a009 21679
    • (1977) Biochemistry , vol.16 , pp. 5217-5220
    • Matthews, J.C.1    Hori, K.2    Cormier, M.J.3
  • 7
    • 0030133674 scopus 로고    scopus 로고
    • Shining the light: The mechanism of the bioluminescence reaction of calcium-binding photoproteins
    • 10.1016/S1074-5521(96)90116-7. 8807862
    • Shining the light: the mechanism of the bioluminescence reaction of calcium-binding photoproteins. Y Ohmiya T Hirano, Chem Biol 1996 3 337 347 10.1016/S1074-5521(96)90116-7 8807862
    • (1996) Chem Biol , vol.3 , pp. 337-347
    • Ohmiya, Y.1    Hirano, T.2
  • 8
    • 0034682381 scopus 로고    scopus 로고
    • The crystal structure of the photoprotein aequorin at 2.3 Å resolution
    • 10.1038/35012659. 10830969
    • The crystal structure of the photoprotein aequorin at 2.3 Å resolution. JF Head S Inouye K Teranishi O Shimomura, Nature 2000 405 372 376 10.1038/35012659 10830969
    • (2000) Nature , vol.405 , pp. 372-376
    • Head, J.F.1    Inouye, S.2    Teranishi, K.3    Shimomura, O.4
  • 9
    • 33644560621 scopus 로고    scopus 로고
    • Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state
    • 16467137. 10.1073/pnas.0511142103
    • Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state. ZJ Liu GA Stepanyuk ES Vysotski J Lee SV Markova NP Malikova BC Wang, Proc Natl Acad Sci USA 2006 103 2570 2575 16467137 10.1073/pnas.0511142103
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2570-2575
    • Liu, Z.J.1    Stepanyuk, G.A.2    Vysotski, E.S.3    Lee, J.4    Markova, S.V.5    Malikova, N.P.6    Wang, B.C.7
  • 10
    • 0016784122 scopus 로고
    • Regeneration of the photoprotein aequorin
    • 10.1038/256236a0. 239351
    • Regeneration of the photoprotein aequorin. O Shimomura FH Johnson, Nature 1975 256 236 238 10.1038/256236a0 239351
    • (1975) Nature , vol.256 , pp. 236-238
    • Shimomura, O.1    Johnson, F.H.2
  • 11
    • 35948997680 scopus 로고    scopus 로고
    • Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis
    • 17980388
    • Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis. AM Loening TD Fenn SS Gambhir, J Mol Biol 2007 374 1017 1028 17980388
    • (2007) J Mol Biol , vol.374 , pp. 1017-1028
    • Loening, A.M.1    Fenn, T.D.2    Gambhir, S.S.3
  • 12
    • 33748101201 scopus 로고    scopus 로고
    • Consensus guided mutagenesis of Renilla luciferase yields enhanced stability and light output
    • 10.1093/protein/gzl023. 16857694
    • Consensus guided mutagenesis of Renilla luciferase yields enhanced stability and light output. AM Loening TD Fenn AM Wu SS Gambhir, Protein Eng Des Sel 2006 19 391 400 10.1093/protein/gzl023 16857694
    • (2006) Protein Eng des Sel , vol.19 , pp. 391-400
    • Loening, A.M.1    Fenn, T.D.2    Wu, A.M.3    Gambhir, S.S.4
  • 13
    • 41649093617 scopus 로고    scopus 로고
    • Structure-function studies on the active site of the coelenterazine- dependent luciferase from Renilla
    • 10.1110/ps.073355508. 18359861
    • Structure-function studies on the active site of the coelenterazine- dependent luciferase from Renilla. JC Woo MH Howell AG von Arnim, Protein Sci 2008 17 725 735 10.1110/ps.073355508 18359861
    • (2008) Protein Sci , vol.17 , pp. 725-735
    • Woo, J.C.1    Howell, M.H.2    Von Arnim, A.G.3
  • 14
    • 0018786147 scopus 로고
    • An energy transfer protein in coelenterate bioluminescence. Characterization of the Renilla green-fluorescent protein
    • 33175
    • An energy transfer protein in coelenterate bioluminescence. Characterization of the Renilla green-fluorescent protein. WW Ward MJ Cormier, J Biol Chem 1979 254 781 788 33175
    • (1979) J Biol Chem , vol.254 , pp. 781-788
    • Ward, W.W.1    Cormier, M.J.2
  • 15
    • 39049141643 scopus 로고    scopus 로고
    • Coelenterazine-binding protein of Renilla muelleri: CDNA cloning overexpression and characterization as a substrate of luciferase
    • 10.1039/b713109g. 18264586
    • Coelenterazine-binding protein of Renilla muelleri: cDNA cloning overexpression and characterization as a substrate of luciferase. MS Titushin SV Markova LA Frank NP Malikova GA Stepanyuk J Lee ES Vysotski, Photochem Photobiol Sci 2008 7 189 196 10.1039/b713109g 18264586
    • (2008) Photochem Photobiol Sci , vol.7 , pp. 189-196
    • Titushin, M.S.1    Markova, S.V.2    Frank, L.A.3    Malikova, N.P.4    Stepanyuk, G.A.5    Lee, J.6    Vysotski, E.S.7
  • 16
    • 34547627492 scopus 로고    scopus 로고
    • Red-shifted Renilla reniformis luciferase variants for imaging in living subjects
    • 10.1038/nmeth1070. 17618292
    • Red-shifted Renilla reniformis luciferase variants for imaging in living subjects. AM Loening AM Wu SS Gambhir, Nat Methods 2007 4 641 643 10.1038/nmeth1070 17618292
    • (2007) Nat Methods , vol.4 , pp. 641-643
    • Loening, A.M.1    Wu, A.M.2    Gambhir, S.S.3
  • 17
    • 33748595271 scopus 로고    scopus 로고
    • A suite of tools and application notes for in vivo protein interaction assays using bioluminescence resonance energy transfer (BRET)
    • 10.1111/j.1365-313X.2006.02851.x. 16925598
    • A suite of tools and application notes for in vivo protein interaction assays using bioluminescence resonance energy transfer (BRET). C Subramanian J Woo X Cai X Xu S Servick CH Johnson A Nebenführ AG von Arnim, Plant J 2006 48 138 152 10.1111/j.1365-313X.2006.02851.x 16925598
    • (2006) Plant J , vol.48 , pp. 138-152
    • Subramanian, C.1    Woo, J.2    Cai, X.3    Xu, X.4    Servick, S.5    Johnson, C.H.6    Nebenführ, A.7    Von Arnim, A.G.8
  • 18
    • 34547147089 scopus 로고    scopus 로고
    • Imaging protein interactions with bioluminescence resonance energy transfer (BRET) in plant and mammalian cells and tissues
    • 17551013. 10.1073/pnas.0701987104
    • Imaging protein interactions with bioluminescence resonance energy transfer (BRET) in plant and mammalian cells and tissues. X Xu M Soutto Q Xie S Servick C Subramanian AG von Arnim CH Johnson, Proc Natl Acad Sci USA 2007 104 10264 10269 17551013 10.1073/pnas.0701987104
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10264-10269
    • Xu, X.1    Soutto, M.2    Xie, Q.3    Servick, S.4    Subramanian, C.5    Von Arnim, A.G.6    Johnson, C.H.7
  • 19
    • 0026585599 scopus 로고
    • Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins
    • 10.1016/0003-2697(92)90279-G. 1595904
    • Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. H Mach CR Middaugh RV Lewis, Anal Biochem 1992 200 74 80 10.1016/0003-2697(92)90279-G 1595904
    • (1992) Anal Biochem , vol.200 , pp. 74-80
    • MacH, H.1    Middaugh, C.R.2    Lewis, R.V.3
  • 20
    • 13844278292 scopus 로고    scopus 로고
    • Interchange of aequorin and obelin bioluminescence color is determined by substitution of one active site residue of each photoprotein
    • 10.1016/j.febslet.2005.01.004. 15710383
    • Interchange of aequorin and obelin bioluminescence color is determined by substitution of one active site residue of each photoprotein. GA Stepanyuk S Golz SV Markova LA Frank J Lee ES Vysotski, FEBS Lett 2005 579 1008 1014 10.1016/j.febslet.2005.01.004 15710383
    • (2005) FEBS Lett , vol.579 , pp. 1008-1014
    • Stepanyuk, G.A.1    Golz, S.2    Markova, S.V.3    Frank, L.A.4    Lee, J.5    Vysotski, E.S.6
  • 21
    • 0018803836 scopus 로고
    • Renilla reniformis bioluminescence: Luciferase-catalyzed production of nonradiating excited states from luciferin analogues and elucidation of the excited state species involved in energy transfer to Renilla green fluorescent protein
    • 10.1021/bi00578a011. 36127
    • Renilla reniformis bioluminescence: luciferase-catalyzed production of nonradiating excited states from luciferin analogues and elucidation of the excited state species involved in energy transfer to Renilla green fluorescent protein. RC Hart JC Matthews K Hori MJ Cormier, Biochemistry 1979 18 2204 2210 10.1021/bi00578a011 36127
    • (1979) Biochemistry , vol.18 , pp. 2204-2210
    • Hart, R.C.1    Matthews, J.C.2    Hori, K.3    Cormier, M.J.4
  • 22
    • 0028939743 scopus 로고
    • Cause of spectral variation in the luminescence of semisynthetic aequorins
    • 7887908
    • Cause of spectral variation in the luminescence of semisynthetic aequorins. O Shimomura, Biochem J 1995 306 537 543 7887908
    • (1995) Biochem J , vol.306 , pp. 537-543
    • Shimomura, O.1
  • 23
    • 2942659225 scopus 로고    scopus 로고
    • 2+-regulated photoproteins: Structural insight into the bioluminescence mechanism
    • 10.1021/ar0400037. 15196050
    • 2+-regulated photoproteins: structural insight into the bioluminescence mechanism. ES Vysotski J Lee, Acc Chem Res 2004 37 405 415 10.1021/ar0400037 15196050
    • (2004) Acc Chem Res , vol.37 , pp. 405-415
    • Vysotski, E.S.1    Lee, J.2
  • 24
    • 34547619629 scopus 로고    scopus 로고
    • Luciferase-YFP fusion tag with enhanced emission for single-cell luminescence imaging
    • 10.1038/nmeth1069. 17618293
    • Luciferase-YFP fusion tag with enhanced emission for single-cell luminescence imaging. H Hoshino Y Nakajima Y Ohmiya, Nat Methods 2007 4 637 639 10.1038/nmeth1069 17618293
    • (2007) Nat Methods , vol.4 , pp. 637-639
    • Hoshino, H.1    Nakajima, Y.2    Ohmiya, Y.3
  • 25
    • 0024386798 scopus 로고
    • Dynamic structural and regulatory aspects of lambda site-specific recombination
    • 2528323
    • Dynamic structural and regulatory aspects of lambda site-specific recombination. A Landy, Annu Rev Biochem 1989 58 913 949 2528323
    • (1989) Annu Rev Biochem , vol.58 , pp. 913-949
    • Landy, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.