메뉴 건너뛰기




Volumn 7, Issue 5, 2003, Pages 557-562

Mechanisms of protein fluorophore formation and engineering

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT DYE; GREEN FLUORESCENT PROTEIN; PROTEIN; PROTEIN DSRED; TRIPEPTIDE; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN;

EID: 0142138258     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(03)00097-8     Document Type: Review
Times cited : (53)

References (25)
  • 1
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67:1998;509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 4
    • 0036823335 scopus 로고    scopus 로고
    • Green fluorescent protein-like proteins in reef Anthozoa animals
    • Miyawaki A. Green fluorescent protein-like proteins in reef Anthozoa animals. Cell Struct. Funct. 27:2002;343-347.
    • (2002) Cell Struct. Funct , vol.27 , pp. 343-347
    • Miyawaki, A.1
  • 5
    • 84984752143 scopus 로고    scopus 로고
    • Negotiating the speed bumps to fluorescence
    • Remington S.J. Negotiating the speed bumps to fluorescence. Nat. Biotechnol. 20:2002;28-29.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 28-29
    • Remington, S.J.1
  • 7
    • 0033674629 scopus 로고    scopus 로고
    • The structural basis for red fluorescence in the tetrameric GFP homolog DsRed
    • Wall M.A., Socolich M., Ranganathan R. The structural basis for red fluorescence in the tetrameric GFP homolog DsRed. Nat. Struct. Biol. 7:2000;1133-1138.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1133-1138
    • Wall, M.A.1    Socolich, M.2    Ranganathan, R.3
  • 10
    • 0031006611 scopus 로고    scopus 로고
    • Chromophore formation in green fluorescent protein
    • Reid B.G., Flynn G.C. Chromophore formation in green fluorescent protein. Biochemistry. 36:1997;6786-6791.
    • (1997) Biochemistry , vol.36 , pp. 6786-6791
    • Reid, B.G.1    Flynn, G.C.2
  • 11
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent proteins
    • Baird G.S., Zacharias D.A., Tsien R.Y. Circular permutation and receptor insertion within green fluorescent proteins. Proc. Natl. Acad. Sci. USA. 96:1999;11241-11246.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 13
    • 0037184962 scopus 로고    scopus 로고
    • Crystal structure of Venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity
    • Rekas A., Alattia J.-R., Nagai T., Miyawaki A., Ikura M. Crystal structure of Venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity. J. Biol. Chem. 277:2002;50573-50578.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50573-50578
    • Rekas, A.1    Alattia, J.-R.2    Nagai, T.3    Miyawaki, A.4    Ikura, M.5
  • 14
    • 0035957110 scopus 로고    scopus 로고
    • Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer
    • Mizuno H., Sawano A., Eli P., Hama H., Miyawaki A. Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer. Biochemistry. 40:2001;2502-2510.
    • (2001) Biochemistry , vol.40 , pp. 2502-2510
    • Mizuno, H.1    Sawano, A.2    Eli, P.3    Hama, H.4    Miyawaki, A.5
  • 15
    • 0034710920 scopus 로고    scopus 로고
    • Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral
    • Baird G.S., Zacharias D.A., Tsien R.Y. Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. USA. 99:2000;11984-11989.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11984-11989
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 16
    • 0037077713 scopus 로고    scopus 로고
    • Oligomerization of DsRed is required for the generation of a functional red fluorescent chromophore
    • Sacchetti A., Subramaniam V., Jovin T.M., Alberti S. Oligomerization of DsRed is required for the generation of a functional red fluorescent chromophore. FEBS Lett. 525:2002;13-19.
    • (2002) FEBS Lett. , vol.525 , pp. 13-19
    • Sacchetti, A.1    Subramaniam, V.2    Jovin, T.M.3    Alberti, S.4
  • 17
    • 0037062424 scopus 로고    scopus 로고
    • A monomeric red fluorescent protein
    • Campbell R.E., Tour O., Palmer A.E., Steinbach P.A., Baird G.S., Zacharias D.A., Tsien R.Y. A monomeric red fluorescent protein. Proc. Natl. Acad. Sci. USA. 99:2002;7877-7882 In this paper, the suitability of the monomeric DsRed, mRFP1, for protein tagging was demonstrated by fusion to the gap junction protein Cx43. Whereas Cx43-DsRed fusion resulted in aggregation in the perinuclear region, Cx43-mRFP1 created functional gap junctions that were stained brightly red.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7877-7882
    • Campbell, R.E.1    Tour, O.2    Palmer, A.E.3    Steinbach, P.A.4    Baird, G.S.5    Zacharias, D.A.6    Tsien, R.Y.7
  • 18
    • 0036138545 scopus 로고    scopus 로고
    • Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed)
    • Bevis B.J., Glick B.S. Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed). Nat. Biotechnol. 20:2002;83-87 Over 100 000 bacterial colonies containing a library of mutated DsRed genes were illuminated by a slide projector, and red emission was detected through goggles covered with filters that allow visualization of all visible wavelengths greater than the cut-on wavelength. A flow cytometer was also used for further characterization of the selected clones.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 83-87
    • Bevis, B.J.1    Glick, B.S.2
  • 19
    • 0037040893 scopus 로고    scopus 로고
    • Analysis of DsRed mutants. Space around the fluorophore accelerates fluorescence development
    • Terskikh A.V., Fradkov A.F., Zaraisky A.G., Kajava A.V., Angres B. Analysis of DsRed mutants. Space around the fluorophore accelerates fluorescence development. J. Biol. Chem. 277:2002;7633-7636 On the basis of the analysis of the three-dimensional structure of DsRed, it has been hypothesized that the availability of space around the chromophore is crucial for fast fluorescence development and complete chromophore modification. This mutagenesis study also led to the generation of E5, the fluorescent timer.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7633-7636
    • Terskikh, A.V.1    Fradkov, A.F.2    Zaraisky, A.G.3    Kajava, A.V.4    Angres, B.5
  • 21
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson G.H., Lippincott-Schwartz J. A photoactivatable GFP for selective photolabeling of proteins and cells. Science. 297:2002;1873-1877 PA-GFP was engineered by improving the natural photoconversion of wild-type Aequorea GFP. PA-GFP can be used as an optical highlighter to mark proteins, organelles and cells of interest, contrasting with conventional fluorescence recovery after photobleaching (FRAP) techniques.
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 22
    • 0036140797 scopus 로고    scopus 로고
    • Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222
    • van Thor J.J., Gensch T., Hellinger K.J., Johnson L.N. Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222. Nat. Struct. Biol. 9:2002;37-41 Oxidative decarboxylation of a γ-carboxylate, which is reported in this paper, may represent a new type of posttranslational modification driven by light.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 37-41
    • Van Thor, J.J.1    Gensch, T.2    Hellinger, K.J.3    Johnson, L.N.4
  • 23
    • 0036789916 scopus 로고    scopus 로고
    • An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein
    • Ando R., Hama H., Yamamoto-Hino M., Mizuno H., Miyawaki A. An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein. Proc. Natl. Acad. Sci. USA. 99:2002;12651-12656 Kaede, a photoconvertible FP, was expressed in a dense culture of neurons and glial cells with entangled long processes, which made it difficult to visualize individual cells. Focusing a pulse of violet light on the body of a neuron produced red-emitting Kaede, which spread over the entire cell, enabling discrimination of its axon and dendrites from those belonging to other cells.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12651-12656
    • Ando, R.1    Hama, H.2    Yamamoto-Hino, M.3    Mizuno, H.4    Miyawaki, A.5
  • 25
    • 0347928662 scopus 로고    scopus 로고
    • Kindling fluorescent proteins for precise in vivo photolabeling
    • Chudakov D.M., Belousov V.V., Zaraisky A.G., Novoselov V.V., Staroverov D.B., Zorov D.B., Lukyanov S., Lukyanov K.A. Kindling fluorescent proteins for precise in vivo photolabeling. Nat. Biotechnol. 21:2003;191-194 Photoactivated (kindled) KFP1 displays relatively low fluorescence quantum yield. The green light (∼532 nm) used to photoactivate this molecule, however, is far less stressful to cells than the UV or violet light (∼400 nm) required to photoactivate PA-GFP or Kaede.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 191-194
    • Chudakov, D.M.1    Belousov, V.V.2    Zaraisky, A.G.3    Novoselov, V.V.4    Staroverov, D.B.5    Zorov, D.B.6    Lukyanov, S.7    Lukyanov, K.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.