Evaluation of fluorophores to label SNAP-tag fused proteins for multicolor single-molecule tracking microscopy in live cells
Single-molecule tracking has become a widely used technique for studying protein dynamics and their organization in the complex environment of the cell. In particular, the spatiotemporal distribution of membrane receptors is an active field of study due to its putative role in the regulation of sign...
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| Veröffentlicht in: | Biophysical journal Jg. 107; H. 4; S. 803 |
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19.08.2014
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| Abstract | Single-molecule tracking has become a widely used technique for studying protein dynamics and their organization in the complex environment of the cell. In particular, the spatiotemporal distribution of membrane receptors is an active field of study due to its putative role in the regulation of signal transduction. The SNAP-tag is an intrinsically monovalent and highly specific genetic tag for attaching a fluorescent label to a protein of interest. Little information is currently available on the choice of optimal fluorescent dyes for single-molecule microscopy utilizing the SNAP-tag labeling system. We surveyed 6 green and 16 red excitable dyes for their suitability in single-molecule microscopy of SNAP-tag fusion proteins in live cells. We determined the nonspecific binding levels and photostability of these dye conjugates when bound to a SNAP-tag fused membrane protein in live cells. We found that only a limited subset of the dyes tested is suitable for single-molecule tracking microscopy. The results show that a careful choice of the dye to conjugate to the SNAP-substrate to label SNAP-tag fusion proteins is very important, as many dyes suffer from either rapid photobleaching or high nonspecific staining. These characteristics appear to be unpredictable, which motivated the need to perform the systematic survey presented here. We have developed a protocol for evaluating the best dyes, and for the conditions that we evaluated, we find that Dy 549 and CF 640 are the best choices tested for single-molecule tracking. Using an optimal dye pair, we also demonstrate the possibility of dual-color single-molecule imaging of SNAP-tag fusion proteins. This survey provides an overview of the photophysical and imaging properties of a range of SNAP-tag fluorescent substrates, enabling the selection of optimal dyes and conditions for single-molecule imaging of SNAP-tagged fusion proteins in eukaryotic cell lines. |
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| AbstractList | Single-molecule tracking has become a widely used technique for studying protein dynamics and their organization in the complex environment of the cell. In particular, the spatiotemporal distribution of membrane receptors is an active field of study due to its putative role in the regulation of signal transduction. The SNAP-tag is an intrinsically monovalent and highly specific genetic tag for attaching a fluorescent label to a protein of interest. Little information is currently available on the choice of optimal fluorescent dyes for single-molecule microscopy utilizing the SNAP-tag labeling system. We surveyed 6 green and 16 red excitable dyes for their suitability in single-molecule microscopy of SNAP-tag fusion proteins in live cells. We determined the nonspecific binding levels and photostability of these dye conjugates when bound to a SNAP-tag fused membrane protein in live cells. We found that only a limited subset of the dyes tested is suitable for single-molecule tracking microscopy. The results show that a careful choice of the dye to conjugate to the SNAP-substrate to label SNAP-tag fusion proteins is very important, as many dyes suffer from either rapid photobleaching or high nonspecific staining. These characteristics appear to be unpredictable, which motivated the need to perform the systematic survey presented here. We have developed a protocol for evaluating the best dyes, and for the conditions that we evaluated, we find that Dy 549 and CF 640 are the best choices tested for single-molecule tracking. Using an optimal dye pair, we also demonstrate the possibility of dual-color single-molecule imaging of SNAP-tag fusion proteins. This survey provides an overview of the photophysical and imaging properties of a range of SNAP-tag fluorescent substrates, enabling the selection of optimal dyes and conditions for single-molecule imaging of SNAP-tagged fusion proteins in eukaryotic cell lines. Single-molecule tracking has become a widely used technique for studying protein dynamics and their organization in the complex environment of the cell. In particular, the spatiotemporal distribution of membrane receptors is an active field of study due to its putative role in the regulation of signal transduction. The SNAP-tag is an intrinsically monovalent and highly specific genetic tag for attaching a fluorescent label to a protein of interest. Little information is currently available on the choice of optimal fluorescent dyes for single-molecule microscopy utilizing the SNAP-tag labeling system. We surveyed 6 green and 16 red excitable dyes for their suitability in single-molecule microscopy of SNAP-tag fusion proteins in live cells. We determined the nonspecific binding levels and photostability of these dye conjugates when bound to a SNAP-tag fused membrane protein in live cells. We found that only a limited subset of the dyes tested is suitable for single-molecule tracking microscopy. The results show that a careful choice of the dye to conjugate to the SNAP-substrate to label SNAP-tag fusion proteins is very important, as many dyes suffer from either rapid photobleaching or high nonspecific staining. These characteristics appear to be unpredictable, which motivated the need to perform the systematic survey presented here. We have developed a protocol for evaluating the best dyes, and for the conditions that we evaluated, we find that Dy 549 and CF 640 are the best choices tested for single-molecule tracking. Using an optimal dye pair, we also demonstrate the possibility of dual-color single-molecule imaging of SNAP-tag fusion proteins. This survey provides an overview of the photophysical and imaging properties of a range of SNAP-tag fluorescent substrates, enabling the selection of optimal dyes and conditions for single-molecule imaging of SNAP-tagged fusion proteins in eukaryotic cell lines.Single-molecule tracking has become a widely used technique for studying protein dynamics and their organization in the complex environment of the cell. In particular, the spatiotemporal distribution of membrane receptors is an active field of study due to its putative role in the regulation of signal transduction. The SNAP-tag is an intrinsically monovalent and highly specific genetic tag for attaching a fluorescent label to a protein of interest. Little information is currently available on the choice of optimal fluorescent dyes for single-molecule microscopy utilizing the SNAP-tag labeling system. We surveyed 6 green and 16 red excitable dyes for their suitability in single-molecule microscopy of SNAP-tag fusion proteins in live cells. We determined the nonspecific binding levels and photostability of these dye conjugates when bound to a SNAP-tag fused membrane protein in live cells. We found that only a limited subset of the dyes tested is suitable for single-molecule tracking microscopy. The results show that a careful choice of the dye to conjugate to the SNAP-substrate to label SNAP-tag fusion proteins is very important, as many dyes suffer from either rapid photobleaching or high nonspecific staining. These characteristics appear to be unpredictable, which motivated the need to perform the systematic survey presented here. We have developed a protocol for evaluating the best dyes, and for the conditions that we evaluated, we find that Dy 549 and CF 640 are the best choices tested for single-molecule tracking. Using an optimal dye pair, we also demonstrate the possibility of dual-color single-molecule imaging of SNAP-tag fusion proteins. This survey provides an overview of the photophysical and imaging properties of a range of SNAP-tag fluorescent substrates, enabling the selection of optimal dyes and conditions for single-molecule imaging of SNAP-tagged fusion proteins in eukaryotic cell lines. |
| Author | Corrêa, Jr, Ivan R Ibach, Jenny Sonntag, Michael H Brunsveld, Luc Kanger, Johannes S Subramaniam, Vinod Bosch, Peter J |
| Author_xml | – sequence: 1 givenname: Peter J surname: Bosch fullname: Bosch, Peter J organization: Nanobiophysics, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands – sequence: 2 givenname: Ivan R surname: Corrêa, Jr fullname: Corrêa, Jr, Ivan R organization: New England Biolabs, Ipswich, Massachusetts – sequence: 3 givenname: Michael H surname: Sonntag fullname: Sonntag, Michael H organization: Laboratory of Chemical Biology, Department of Biomedical Engineering, and Institute of Complex Molecular Systems, Eindhoven University of Technology, Eindhoven, The Netherlands – sequence: 4 givenname: Jenny surname: Ibach fullname: Ibach, Jenny organization: Max Planck Institute of Molecular Physiology, Dortmund, Germany – sequence: 5 givenname: Luc surname: Brunsveld fullname: Brunsveld, Luc organization: Laboratory of Chemical Biology, Department of Biomedical Engineering, and Institute of Complex Molecular Systems, Eindhoven University of Technology, Eindhoven, The Netherlands – sequence: 6 givenname: Johannes S surname: Kanger fullname: Kanger, Johannes S organization: Nanobiophysics, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands – sequence: 7 givenname: Vinod surname: Subramaniam fullname: Subramaniam, Vinod email: subramaniam@amolf.nl organization: Nanobiophysics, MESA+ Institute for Nanotechnology and MIRA Institute for Biomedical Technology and Technical Medicine, University of Twente, Enschede, The Netherlands. Electronic address: subramaniam@amolf.nl |
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| References | 23431983 - Curr Pharm Des. 2013;19(30):5414-20 21765402 - Nat Biotechnol. 2011 Aug;29(8):757-61 11389468 - Nat Rev Mol Cell Biol. 2001 Jun;2(6):444-56 24122039 - Nat Methods. 2013 Dec;10(12):1203-5 21499265 - Nat Chem Biol. 2011 Jun;7(6):375-83 10449539 - J Histochem Cytochem. 1999 Sep;47(9):1179-88 11325739 - Biophys J. 2001 May;80(5):2396-408 11023923 - Biophys J. 2000 Oct;79(4):2188-98 20815338 - Anal Chem. 2010 Oct 1;82(19):8186-93 15681376 - Science. 2005 Jan 28;307(5709):538-44 24411259 - Biophys J. 2014 Jan 7;106(1):272-8 20130139 - J Cell Sci. 2010 Feb 1;123(Pt 3):309-20 21793150 - Chembiochem. 2011 Sep 19;12(14):2217-26 16614209 - Science. 2006 Apr 14;312(5771):217-24 18469015 - J Cell Sci. 2008 May 15;121(Pt 10):1750-7 16113650 - EMBO Rep. 2005 Oct;6(10):942-8 23095089 - J Am Chem Soc. 2012 Nov 21;134(46):19026-34 21700215 - Chem Biol. 2011 Jun 24;18(6):805-15 20495582 - Nat Rev Mol Cell Biol. 2010 Jun;11(6):414-26 18634880 - Methods. 2008 Oct;46(2):131-40 6783667 - J Cell Biol. 1981 Mar;88(3):526-35 16299475 - Nat Methods. 2005 Dec;2(12):905-9 15226507 - Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):9955-9 23267088 - Proc Natl Acad Sci U S A. 2013 Jan 8;110(2):743-8 21191367 - Nat Methods. 2011 Jan;8(1):7-9 19416318 - Dev Med Child Neurol. 2009 Nov;51(11):917-22 22519662 - Nano Lett. 2012 May 9;12(5):2619-24 22004174 - ACS Chem Biol. 2012 Jan 20;7(1):139-49 21348524 - Bioconjug Chem. 2011 Mar 16;22(3):510-7 22056676 - Nat Methods. 2011 Dec;8(12):1027-36 22669501 - Ann Biomed Eng. 2012 Nov;40(11):2307-18 24015360 - Elife. 2013;2:e01008 19134478 - Biophys J. 2009 Jan;96(1):226-37 12469133 - Nat Biotechnol. 2003 Jan;21(1):86-9 23344448 - Nat Chem. 2013 Feb;5(2):132-9 22231401 - Nat Struct Mol Biol. 2012 Feb;19(2):193-200 18604216 - Nat Methods. 2008 Aug;5(8):687-94 23129641 - Proc Natl Acad Sci U S A. 2012 Dec 4;109(49):E3340-9 22654058 - Science. 2012 Jun 1;336(6085):1164-8 21393538 - Science. 2011 Mar 11;331(6022):1289-95 18620858 - Trends Cell Biol. 2008 Aug;18(8):364-71 21941275 - Nat Rev Mol Cell Biol. 2011 Oct;12(10):656-68 22543373 - Nat Methods. 2012 May;9(5):428-9 20940297 - J Biol Chem. 2010 Dec 10;285(50):39481-9 23717596 - PLoS One. 2013;8(5):e64320 18805933 - Biophys J. 2008 Dec 15;95(12):5988-6001 23169684 - Angew Chem Int Ed Engl. 2013 Jan 7;52(2):691-4 9251823 - Biophys J. 1997 Aug;73(2):1073-80 18412538 - Annu Rev Biochem. 2008;77:51-76 14695280 - Biophys J. 2004 Jan;86(1 Pt 1):384-94 22061422 - J Neurosci Methods. 2012 Feb 15;204(1):82-6 21420957 - FEBS Lett. 2011 Apr 20;585(8):1185-90 25099798 - Biophys J. 2014 Aug 5;107(3):588-98 23292935 - Proc Natl Acad Sci U S A. 2013 Jan 22;110(4):1285-90 23850281 - Curr Biol. 2013 Jul 22;23(14):1373-9 15869394 - Annu Rev Biophys Biomol Struct. 2005;34:351-78 21833373 - Biomed Opt Express. 2011 Aug 1;2(8):2364-71 18425138 - Nat Methods. 2008 May;5(5):397-9 23200186 - Trends Biochem Sci. 2013 Jan;38(1):30-7 20354518 - Nat Methods. 2010 Apr;7(4):275-85 23331306 - Annu Rev Phys Chem. 2013;64:459-80 18291317 - Chem Biol. 2008 Feb;15(2):128-36 22020299 - Nat Struct Mol Biol. 2011 Nov;18(11):1244-9 20364146 - Nat Methods. 2010 May;7(5):373-5 9241424 - Annu Rev Biophys Biomol Struct. 1997;26:373-99 14704683 - Nat Biotechnol. 2004 Feb;22(2):198-203 11751315 - Biophys J. 2002 Jan;82(1 Pt 1):274-84 16829981 - Nat Rev Mol Cell Biol. 2006 Jul;7(7):505-16 22891263 - J Cell Biol. 2012 Aug 20;198(4):591-605 10707088 - Nat Cell Biol. 2000 Mar;2(3):168-72 23065903 - Science. 2012 Nov 2;338(6107):662-5 19362843 - Trends Biochem Sci. 2009 May;34(5):234-43 |
| References_xml | – reference: 24015360 - Elife. 2013;2:e01008 – reference: 16113650 - EMBO Rep. 2005 Oct;6(10):942-8 – reference: 21793150 - Chembiochem. 2011 Sep 19;12(14):2217-26 – reference: 22891263 - J Cell Biol. 2012 Aug 20;198(4):591-605 – reference: 11325739 - Biophys J. 2001 May;80(5):2396-408 – reference: 16299475 - Nat Methods. 2005 Dec;2(12):905-9 – reference: 22519662 - Nano Lett. 2012 May 9;12(5):2619-24 – reference: 23169684 - Angew Chem Int Ed Engl. 2013 Jan 7;52(2):691-4 – reference: 16829981 - Nat Rev Mol Cell Biol. 2006 Jul;7(7):505-16 – reference: 22669501 - Ann Biomed Eng. 2012 Nov;40(11):2307-18 – reference: 18805933 - Biophys J. 2008 Dec 15;95(12):5988-6001 – reference: 23431983 - Curr Pharm Des. 2013;19(30):5414-20 – reference: 18469015 - J Cell Sci. 2008 May 15;121(Pt 10):1750-7 – reference: 22004174 - ACS Chem Biol. 2012 Jan 20;7(1):139-49 – reference: 6783667 - J Cell Biol. 1981 Mar;88(3):526-35 – reference: 22056676 - Nat Methods. 2011 Dec;8(12):1027-36 – reference: 21420957 - FEBS Lett. 2011 Apr 20;585(8):1185-90 – reference: 23129641 - Proc Natl Acad Sci U S A. 2012 Dec 4;109(49):E3340-9 – reference: 21499265 - Nat Chem Biol. 2011 Jun;7(6):375-83 – reference: 23344448 - Nat Chem. 2013 Feb;5(2):132-9 – reference: 20815338 - Anal Chem. 2010 Oct 1;82(19):8186-93 – reference: 12469133 - Nat Biotechnol. 2003 Jan;21(1):86-9 – reference: 22061422 - J Neurosci Methods. 2012 Feb 15;204(1):82-6 – reference: 20940297 - J Biol Chem. 2010 Dec 10;285(50):39481-9 – reference: 18620858 - Trends Cell Biol. 2008 Aug;18(8):364-71 – reference: 20495582 - Nat Rev Mol Cell Biol. 2010 Jun;11(6):414-26 – reference: 14695280 - Biophys J. 2004 Jan;86(1 Pt 1):384-94 – reference: 21833373 - Biomed Opt Express. 2011 Aug 1;2(8):2364-71 – reference: 23095089 - J Am Chem Soc. 2012 Nov 21;134(46):19026-34 – reference: 21393538 - Science. 2011 Mar 11;331(6022):1289-95 – reference: 15226507 - Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):9955-9 – reference: 11751315 - Biophys J. 2002 Jan;82(1 Pt 1):274-84 – reference: 21765402 - Nat Biotechnol. 2011 Aug;29(8):757-61 – reference: 19416318 - Dev Med Child Neurol. 2009 Nov;51(11):917-22 – reference: 23267088 - Proc Natl Acad Sci U S A. 2013 Jan 8;110(2):743-8 – reference: 19362843 - Trends Biochem Sci. 2009 May;34(5):234-43 – reference: 9241424 - Annu Rev Biophys Biomol Struct. 1997;26:373-99 – reference: 18604216 - Nat Methods. 2008 Aug;5(8):687-94 – reference: 23065903 - Science. 2012 Nov 2;338(6107):662-5 – reference: 25099798 - Biophys J. 2014 Aug 5;107(3):588-98 – reference: 19134478 - Biophys J. 2009 Jan;96(1):226-37 – reference: 16614209 - Science. 2006 Apr 14;312(5771):217-24 – reference: 10707088 - Nat Cell Biol. 2000 Mar;2(3):168-72 – reference: 20130139 - J Cell Sci. 2010 Feb 1;123(Pt 3):309-20 – reference: 21700215 - Chem Biol. 2011 Jun 24;18(6):805-15 – reference: 22543373 - Nat Methods. 2012 May;9(5):428-9 – reference: 15869394 - Annu Rev Biophys Biomol Struct. 2005;34:351-78 – reference: 18425138 - Nat Methods. 2008 May;5(5):397-9 – reference: 18412538 - Annu Rev Biochem. 2008;77:51-76 – reference: 9251823 - Biophys J. 1997 Aug;73(2):1073-80 – reference: 24411259 - Biophys J. 2014 Jan 7;106(1):272-8 – reference: 23200186 - Trends Biochem Sci. 2013 Jan;38(1):30-7 – reference: 11023923 - Biophys J. 2000 Oct;79(4):2188-98 – reference: 21941275 - Nat Rev Mol Cell Biol. 2011 Oct;12(10):656-68 – reference: 22020299 - Nat Struct Mol Biol. 2011 Nov;18(11):1244-9 – reference: 23850281 - Curr Biol. 2013 Jul 22;23(14):1373-9 – reference: 10449539 - J Histochem Cytochem. 1999 Sep;47(9):1179-88 – reference: 24122039 - Nat Methods. 2013 Dec;10(12):1203-5 – reference: 23331306 - Annu Rev Phys Chem. 2013;64:459-80 – reference: 14704683 - Nat Biotechnol. 2004 Feb;22(2):198-203 – reference: 18291317 - Chem Biol. 2008 Feb;15(2):128-36 – reference: 11389468 - Nat Rev Mol Cell Biol. 2001 Jun;2(6):444-56 – reference: 22654058 - Science. 2012 Jun 1;336(6085):1164-8 – reference: 21191367 - Nat Methods. 2011 Jan;8(1):7-9 – reference: 20364146 - Nat Methods. 2010 May;7(5):373-5 – reference: 20354518 - Nat Methods. 2010 Apr;7(4):275-85 – reference: 23292935 - Proc Natl Acad Sci U S A. 2013 Jan 22;110(4):1285-90 – reference: 21348524 - Bioconjug Chem. 2011 Mar 16;22(3):510-7 – reference: 22231401 - Nat Struct Mol Biol. 2012 Feb;19(2):193-200 – reference: 15681376 - Science. 2005 Jan 28;307(5709):538-44 – reference: 23717596 - PLoS One. 2013;8(5):e64320 – reference: 18634880 - Methods. 2008 Oct;46(2):131-40 |
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| SubjectTerms | Cell Line, Tumor Female Fluorescent Dyes - chemistry HeLa Cells Humans Microscopy, Fluorescence - methods Photobleaching Photochemical Processes Proteins - chemistry Proteins - metabolism |
| Title | Evaluation of fluorophores to label SNAP-tag fused proteins for multicolor single-molecule tracking microscopy in live cells |
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