Fiber-optic system for monitoring fast photoactivation dynamics of optical highlighter fluorescent proteins

doi:10.1364/BOE.2.002117

Fiber-optic system for monitoring fast photoactivation dynamics of optical highlighter fluorescent proteins

Zhiguo Pei, Lingsong Qin, Zhihong Zhang, Shaoqun Zeng, and Zhen-Li Huang »View Author Affiliations

Biomedical Optics Express, Vol. 2, Issue 8, pp. 2117-2125 (2011)
http://dx.doi.org/10.1364/BOE.2.002117

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Abstract
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Abstract

Characterizing the photoactivation performance of optical highlighter fluorescent proteins is crucial to the realization of photoactivation localization microscopy. In contrast to those fluorescence-based approaches that require complex data processing and calibration procedures, here we report a simple and quantitative alternative, which relies on the measurement of small absorption spectra changes over time with a fiber-optic system. Using Dronpa as a representative highlighter protein, we have investigated the capacity of this system in monitoring the fast photoactivation process.

OCIS Codes
(120.6200) Instrumentation, measurement, and metrology : Spectrometers and spectroscopic instrumentation
(300.1030) Spectroscopy : Absorption

ToC Category:
Optical Biophysics

History
Original Manuscript: May 9, 2011
Revised Manuscript: June 28, 2011
Manuscript Accepted: July 1, 2011
Published: July 1, 2011

Citation
Zhiguo Pei, Lingsong Qin, Zhihong Zhang, Shaoqun Zeng, and Zhen-Li Huang, "Fiber-optic system for monitoring fast photoactivation dynamics of optical highlighter fluorescent proteins," Biomed. Opt. Express 2, 2117-2125 (2011)
http://www.opticsinfobase.org/boe/abstract.cfm?URI=boe-2-8-2117

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References

S. W. Hell, “Far-field optical nanoscopy,” Science 316(5828), 1153–1158 (2007). [CrossRef] [PubMed]
B. Huang, H. Babcock, and X. Zhuang, “Breaking the diffraction barrier: super-resolution imaging of cells,” Cell 143(7), 1047–1058 (2010). [CrossRef] [PubMed]
E. Betzig, G. H. Patterson, R. Sougrat, O. W. Lindwasser, S. Olenych, J. S. Bonifacino, M. W. Davidson, J. Lippincott-Schwartz, and H. F. Hess, “Imaging intracellular fluorescent proteins at nanometer resolution,” Science 313(5793), 1642–1645 (2006). [CrossRef] [PubMed]
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P. Kanchanawong, G. Shtengel, A. M. Pasapera, E. B. Ramko, M. W. Davidson, H. F. Hess, and C. M. Waterman, “Nanoscale architecture of integrin-based cell adhesions,” Nature 468(7323), 580–584 (2010). [CrossRef] [PubMed]
J. Liu, Z. G. Pei, L. Wang, Z. H. Zhang, S. Q. Zeng, and Z. L. Huang, “A straightforward and quantitative approach for characterizing the photoactivation performance of optical highlighter fluorescent proteins,” Appl. Phys. Lett. 97(20), 203701 (2010). [CrossRef]
F. V. Subach, G. H. Patterson, S. Manley, J. M. Gillette, J. Lippincott-Schwartz, and V. V. Verkhusha, “Photoactivatable mCherry for high-resolution two-color fluorescence microscopy,” Nat. Methods 6(2), 153–159 (2009). [CrossRef] [PubMed]
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R. Ando, H. Mizuno, and A. Miyawaki, “Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting,” Science 306(5700), 1370–1373 (2004). [CrossRef] [PubMed]
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E. Pastrana, “Fast 3D super-resolution fluorescence microscopy,” Nat. Methods 8(1), 46 (2011). [CrossRef]
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“HL-2000 tungsten halogen light sources,” http://www.oceanoptics.com/Products/hl2000.asp , accessed Mar. 2011.
“USB2000+ Miniature Fiber Optic Spectrometer,” http://www.oceanoptics.com/Products/usb2000+.asp , accessed Mar. 2011.
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Adam, V.
Ando, R.
Andresen, M.
Babcock, H.
Betzig, E.
Bonifacino, J. S.
Bourgeois, D.
Carpentier, P.
Darnault, C.
Davidson, M.
Davidson, M. W.
de Rosny, E.
Dedecker, P.
Eggeling, C.
Faro, A. R.
Flors, C.
Galbraith, C. G.
Galbraith, J. A.
Gillette, J. M.
Habuchi, S.
Hell, S. W.
Hess, H. F.
Hofkens, J.
Hotta, J.-i.
Huang, B.
Huang, Z. L.
Jakobs, S.
Kanchanawong, P.
Lindwasser, O. W.
Lippincott-Schwartz, J.
Liu, J.
Manley, S.
Miyawaki, A.
Mizuno, H.
Olenych, S.
Pasapera, A. M.
Pastrana, E.
Patterson, G.
Patterson, G. H.
Pei, Z. G.
Ramko, E. B.
Shroff, H.
Shtengel, G.
Sougrat, R.
Stiel, A. C.
Subach, F. V.
Trowitzsch, S.
Uji-i, H.
Verheijen, W.
Verkhusha, V. V.
Wahl, M. C.
Wang, L.
Waterman, C. M.
Weber, G.
Zeng, S. Q.
Zhang, Z. H.
Zhuang, X.

Annu. Rev. Phys. Chem.

G. Patterson, M. Davidson, S. Manley, and J. Lippincott-Schwartz, “Superresolution imaging using single-molecule localization,” Annu. Rev. Phys. Chem. 61(1), 345–367 (2010). [CrossRef] [PubMed]

Appl. Phys. Lett.

J. Liu, Z. G. Pei, L. Wang, Z. H. Zhang, S. Q. Zeng, and Z. L. Huang, “A straightforward and quantitative approach for characterizing the photoactivation performance of optical highlighter fluorescent proteins,” Appl. Phys. Lett. 97(20), 203701 (2010). [CrossRef]

Cell

B. Huang, H. Babcock, and X. Zhuang, “Breaking the diffraction barrier: super-resolution imaging of cells,” Cell 143(7), 1047–1058 (2010). [CrossRef] [PubMed]

J. Am. Chem. Soc.

C. Flors, J.-i. Hotta, H. Uji-i, P. Dedecker, R. Ando, H. Mizuno, A. Miyawaki, and J. Hofkens, “A stroboscopic approach for fast photoactivation-localization microscopy with Dronpa mutants,” J. Am. Chem. Soc. 129(45), 13970–13977 (2007). [CrossRef] [PubMed]

Nat. Methods

E. Pastrana, “Fast 3D super-resolution fluorescence microscopy,” Nat. Methods 8(1), 46 (2011). [CrossRef]
H. Shroff, C. G. Galbraith, J. A. Galbraith, and E. Betzig, “Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics,” Nat. Methods 5(5), 417–423 (2008). [CrossRef] [PubMed]
F. V. Subach, G. H. Patterson, S. Manley, J. M. Gillette, J. Lippincott-Schwartz, and V. V. Verkhusha, “Photoactivatable mCherry for high-resolution two-color fluorescence microscopy,” Nat. Methods 6(2), 153–159 (2009). [CrossRef] [PubMed]

Nature

P. Kanchanawong, G. Shtengel, A. M. Pasapera, E. B. Ramko, M. W. Davidson, H. F. Hess, and C. M. Waterman, “Nanoscale architecture of integrin-based cell adhesions,” Nature 468(7323), 580–584 (2010). [CrossRef] [PubMed]

Photochem. Photobiol. Sci.

S. Habuchi, P. Dedecker, J.-i. Hotta, C. Flors, R. Ando, H. Mizuno, A. Miyawaki, and J. Hofkens, “Photo-induced protonation/deprotonation in the GFP-like fluorescent protein Dronpa: mechanism responsible for the reversible photoswitching,” Photochem. Photobiol. Sci. 5(6), 567–576 (2006). [CrossRef] [PubMed]
A. R. Faro, V. Adam, P. Carpentier, C. Darnault, D. Bourgeois, and E. de Rosny, “Low-temperature switching by photoinduced protonation in photochromic fluorescent proteins,” Photochem. Photobiol. Sci. 9(2), 254–262 (2010). [CrossRef] [PubMed]

Proc. Natl. Acad. Sci. U.S.A.

S. Habuchi, R. Ando, P. Dedecker, W. Verheijen, H. Mizuno, A. Miyawaki, and J. Hofkens, “Reversible single-molecule photoswitching in the GFP-like fluorescent protein Dronpa,” Proc. Natl. Acad. Sci. U.S.A. 102(27), 9511–9516 (2005). [CrossRef] [PubMed]
M. Andresen, A. C. Stiel, S. Trowitzsch, G. Weber, C. Eggeling, M. C. Wahl, S. W. Hell, and S. Jakobs, “Structural basis for reversible photoswitching in Dronpa,” Proc. Natl. Acad. Sci. U.S.A. 104(32), 13005–13009 (2007). [CrossRef] [PubMed]

Science

S. W. Hell, “Far-field optical nanoscopy,” Science 316(5828), 1153–1158 (2007). [CrossRef] [PubMed]
E. Betzig, G. H. Patterson, R. Sougrat, O. W. Lindwasser, S. Olenych, J. S. Bonifacino, M. W. Davidson, J. Lippincott-Schwartz, and H. F. Hess, “Imaging intracellular fluorescent proteins at nanometer resolution,” Science 313(5793), 1642–1645 (2006). [CrossRef] [PubMed]
R. Ando, H. Mizuno, and A. Miyawaki, “Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting,” Science 306(5700), 1370–1373 (2004). [CrossRef] [PubMed]

Other

Ocean Optics catalog (Ocean Optics, Inc., 2011).
N. Irwin and K. A. Janssen, Molecular Cloning: a Laboratory Manual, 3ed., J. Argentine and N. Irwin, eds. (Cold Spring Harbor Laboratory Press, New York 2001).
“CCD noise sources and signal-to-noise ratio,” http://learn.hamamatsu.com/articles/ccdsnr.html , accessed Mar. 2011.
“HL-2000 tungsten halogen light sources,” http://www.oceanoptics.com/Products/hl2000.asp , accessed Mar. 2011.
“USB2000+ Miniature Fiber Optic Spectrometer,” http://www.oceanoptics.com/Products/usb2000+.asp , accessed Mar. 2011.
S. W. Smith, The Scientist and Engineer's Guide to Digital Signal Processing, 2nd ed. (California Technical Publishing, 2003).

2011, Pastrana, Nat. Methods
2010, Faro, Photochem. Photobiol. Sci.
2010, Huang, Cell
2010, Kanchanawong, Nature
2010, Liu, Appl. Phys. Lett.
2010, Patterson, Annu. Rev. Phys. Chem.
2009, Subach, Nat. Methods
2008, Shroff, Nat. Methods
2007, Hell, Science
2007, Flors, J. Am. Chem. Soc.
2007, Andresen, Proc. Natl. Acad. Sci. U.S.A.
2006, Habuchi, Photochem. Photobiol. Sci.
2006, Betzig, Science
2005, Habuchi, Proc. Natl. Acad. Sci. U.S.A.
2004, Ando, Science

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