Fast Biosynthesis of GFP Molecules: A Single-Molecule Fluorescence Study

被引：40

作者：

Katranidis, Alexandros ^{[1
,2
]}

Atta, Diaa ^{[1
]}

Schlesinger, Ramona ^{[1
]}

Nierhaus, Knud H. ^{[3
]}

Choli-Papadopoulou, Theodora ^{[2
]}

Gregor, Ingo ^{[4
]}

Gerrits, Michael ^{[5
]}

Bueldt, Georg ^{[1
]}

Fitter, Joerg ^{[1
]}

机构：

[1] Forschungszentrum Julich, Mol Biophys ISB 2, D-52425 Julich, Germany

[2] Aristotle Univ Thessaloniki, Biochem Lab, Thessaloniki, Greece

[3] Max Planck Inst Mol Genet, Berlin, Germany

[4] Forschungszentrum Julich, Cellular Biophys ISB 1, D-52425 Julich, Germany

[5] RiNA GmbH, D-14195 Berlin, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 10期

关键词：

fluorescence microscopy; green fluorescent proteins; protein folding; ribosomes; single-molecule studies; FIREFLY LUCIFERASE; PROTEIN-SYNTHESIS; TRANSFER-RNA; RIBOSOME; POLYPEPTIDE; TRANSLATION; CELLS;

D O I：

10.1002/anie.200806070

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

It's not easy being green: Real-time visualization of labeled ribosomes and de novo synthesized green fluorescent protein molecules using single-moleculesensitive fluorescence microscopy demonstrates that the mutant GFPem is produced with a characteristic time of five minutes. Fluorescence of the fastest GFP molecules appears within one minute (see picture).© 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：1758 / 1761

页数：4

共 28 条

[1] Biofunctionalized polymer surfaces exhibiting minimal interaction towards immobilized proteins [J].

Amirgoulova, EV ;

Groll, J ;

Heyes, CD ;

Ameringer, T ;

Röcker, C ;

Möller, M ;

Nienhaus, GU .

CHEMPHYSCHEM, 2004, 5 (04) :552-555

[2] tRNA selection and kinetic proofreading in translation [J].

Blanchard, SC ;

Gonzalez, RL ;

Kim, HD ;

Chu, S ;

Puglisi, JD .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2004, 11 (10) :1008-1014

[3] Tracking unfolding and refolding of single GFPmut2 molecules [J].

Cannone, F ;

Bologna, S ;

Campanini, B ;

Diaspro, A ;

Bettati, S ;

Mozzarelli, A ;

Chirico, G .

BIOPHYSICAL JOURNAL, 2005, 89 (03) :2033-2045

[4] A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates [J].

Clark, PL ;

King, J .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (27) :25411-25420

[5] Simultaneous dual-color and dual-polarization imaging of single molecules [J].

Cognet, L ;

Harms, GS ;

Blab, GA ;

Lommerse, PHM ;

Schmidt, T .

APPLIED PHYSICS LETTERS, 2000, 77 (24) :4052-4054

[6] Molecular Simulations of cotranslational protein folding: Fragment stabilities, folding cooperativity, and trapping in the ribosome [J].

Elcock, Adrian H. .

PLOS COMPUTATIONAL BIOLOGY, 2006, 2 (07) :824-841

[7] The dynamic tunnel [J].

Etchells, SA ;

Hartl, FU .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2004, 11 (05) :391-392

[8] Process of biosynthetic protein folding determines the rapid formation of native structure [J].

Fedorov, AN ;

Baldwin, TO .

JOURNAL OF MOLECULAR BIOLOGY, 1999, 294 (02) :579-586

[9] Cotranslational protein folding [J].

Fedorov, AN ;

Baldwin, TO .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (52) :32715-32718

[10] Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase [J].

Frydman, J ;

Erdjument-Bromage, H ;

Tempst, P ;

Hartl, FU .

NATURE STRUCTURAL BIOLOGY, 1999, 6 (07) :697-705

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