Fast Complementation of Split Fluorescent Protein Triggered by DNA Hybridization
Fluorescent proteins have proven to be excellent reporters and biochemical sensors with a wide range of applications. In a split form, they are not fluorescent, but their fluorescence can be restored by supplementary protein-protein or protein-nucleic acid interactions that reassemble the split poly...
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| Published in: | Proceedings of the National Academy of Sciences - PNAS Vol. 103; no. 7; pp. 2052 - 2056 |
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| Main Authors: | , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
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National Academy of Sciences
14-02-2006
National Acad Sciences |
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| Abstract | Fluorescent proteins have proven to be excellent reporters and biochemical sensors with a wide range of applications. In a split form, they are not fluorescent, but their fluorescence can be restored by supplementary protein-protein or protein-nucleic acid interactions that reassemble the split polypeptides. However, in prior studies, it took hours to restore the fluorescence of a split fluorescent protein because the formation of the protein chromophore slowly occurred de novo concurrently with reassembly. Here we provide evidence that a fluorogenic chromophore can self-catalytically form within an isolated N-terminal fragment of the enhanced green fluorescent protein (EGFP). We show that restoration of the split protein fluorescence can be driven by nucleic acid complementary interactions. In our assay, fluorescence development is fast (within a few minutes) when complementary oligonucleotide-linked fragments of the split EGFP are combined. The ability of our EGFP system to respond quickly to DNA hybridization should be useful for detecting the kinetics of many other types of pairwise interactions both in vitro and in living cells. |
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| AbstractList | Fluorescent proteins have proven to be excellent reporters and biochemical sensors with a wide range of applications. In a split form, they are not fluorescent, but their fluorescence can be restored by supplementary protein-protein or protein-nucleic acid interactions that reassemble the split polypeptides. However, in prior studies, it took hours to restore the fluorescence of a split fluorescent protein because the formation of the protein chromophore slowly occurred de novo concurrently with reassembly. Here we provide evidence that a fluorogenic chromophore can self-catalytically form within an isolated N-terminal fragment of the enhanced green fluorescent protein (EGFP). We show that restoration of the split protein fluorescence can be driven by nucleic acid complementary interactions. In our assay, fluorescence development is fast (within a few minutes) when complementary oligonucleotide-linked fragments of the split EGFP are combined. The ability of our EGFP system to respond quickly to DNA hybridization should be useful for detecting the kinetics of many other types of pairwise interactions both in vitro and in living cells. Fluorescent proteins have proven to be excellent reporters and biochemical sensors with a wide range of applications. In a split form, they are not fluorescent, but their fluorescence can be restored by supplementary protein–protein or protein–nucleic acid interactions that reassemble the split polypeptides. However, in prior studies, it took hours to restore the fluorescence of a split fluorescent protein because the formation of the protein chromophore slowly occurred de novo concurrently with reassembly. Here we provide evidence that a fluorogenic chromophore can self-catalytically form within an isolated N-terminal fragment of the enhanced green fluorescent protein (EGFP). We show that restoration of the split protein fluorescence can be driven by nucleic acid complementary interactions. In our assay, fluorescence development is fast (within a few minutes) when complementary oligonucleotide-linked fragments of the split EGFP are combined. The ability of our EGFP system to respond quickly to DNA hybridization should be useful for detecting the kinetics of many other types of pairwise interactions both in vitro and in living cells. Fluorescent proteins have proven to be excellent reporters and biochemical sensors with a wide range of applications. In a split form, they are not fluorescent, but their fluorescence can be restored by supplementary protein–protein or protein–nucleic acid interactions that reassemble the split polypeptides. However, in prior studies, it took hours to restore the fluorescence of a split fluorescent protein because the formation of the protein chromophore slowly occurred de novo concurrently with reassembly. Here we provide evidence that a fluorogenic chromophore can self-catalytically form within an isolated N-terminal fragment of the enhanced green fluorescent protein (EGFP). We show that restoration of the split protein fluorescence can be driven by nucleic acid complementary interactions. In our assay, fluorescence development is fast (within a few minutes) when complementary oligonucleotide-linked fragments of the split EGFP are combined. The ability of our EGFP system to respond quickly to DNA hybridization should be useful for detecting the kinetics of many other types of pairwise interactions both in vitro and in living cells. split EGFP DNA duplex EGFP reassembly protein folding DMD simulations Fluorescent proteins have proven to be excellent reporters and biochemical sensors with a wide range of applications. In a split form, they are not fluorescent, but their fluorescence can be restored by supplementary protein-protein or protein-nucleic acid interactions that reassemble the split polypeptides. However, in prior studies, it took hours to restore the fluorescence of a split fluorescent protein because the formation of the protein chromophore slowly occurred de novo concurrently with reassembly. Here we provide evidence that a fluorogenic chromophore can self-catalytically form within an isolated N-terminal fragment of the enhanced green fluorescent protein (EGFP). We show that restoration of the split protein fluorescence can be driven by nucleic acid complementary interactions. In our assay, fluorescence development is fast (within a few minutes) when complementary oligonucleotide-linked fragments of the split EGFP are combined. The ability of our EGFP system to respond quickly to DNA hybridization should be useful for detecting the kinetics of many other types of pairwise interactions both in vitro and in living cells. [PUBLICATION ABSTRACT] |
| Author | Demidov, Vadim V. Cantor, Charles R. Dokholyan, Nikolay V. Witte-Hoffmann, Carlos Ding, Feng Yiu, Hung-Wei Yu, Yong Broude, Natalia E. Chalasani, Poornima |
| Author_xml | – sequence: 1 givenname: Vadim V. surname: Demidov fullname: Demidov, Vadim V. – sequence: 2 givenname: Nikolay V. surname: Dokholyan fullname: Dokholyan, Nikolay V. – sequence: 3 givenname: Carlos surname: Witte-Hoffmann fullname: Witte-Hoffmann, Carlos – sequence: 4 givenname: Poornima surname: Chalasani fullname: Chalasani, Poornima – sequence: 5 givenname: Hung-Wei surname: Yiu fullname: Yiu, Hung-Wei – sequence: 6 givenname: Feng surname: Ding fullname: Ding, Feng – sequence: 7 givenname: Yong surname: Yu fullname: Yu, Yong – sequence: 8 givenname: Charles R. surname: Cantor fullname: Cantor, Charles R. – sequence: 9 givenname: Natalia E. surname: Broude fullname: Broude, Natalia E. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16461889$$D View this record in MEDLINE/PubMed |
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| Copyright | Copyright 2006 National Academy of Sciences of the United States of America Copyright National Academy of Sciences Feb 14, 2006 2006 by The National Academy of Sciences of the USA 2006 |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Contributed by Charles R. Cantor, December 22, 2005 Author contributions: V.V.D., N.V.D., C.W.-H., C.R.C., and N.E.B. designed research; V.V.D., N.V.D., C.W.-H., P.C., H.-W.Y., F.D., and Y.Y. performed research; V.V.D., N.V.D., F.D., C.R.C., and N.E.B. analyzed data; and V.V.D., C.R.C., and N.E.B. wrote the paper. |
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| Snippet | Fluorescent proteins have proven to be excellent reporters and biochemical sensors with a wide range of applications. In a split form, they are not... |
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| SubjectTerms | Amino acids Biochemistry Biological Sciences Chromophores Complementation Deoxyribonucleic acid DNA DNA - chemistry Duchenne muscular dystrophy Fluorescence Green Fluorescent Proteins - chemistry Green Fluorescent Proteins - genetics Hybridization Nucleic Acid Hybridization Oligonucleotides Oligonucleotides - chemistry Protein Folding Protein refolding Proteins Sequence Deletion Spectrometry, Fluorescence - methods |
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| Title | Fast Complementation of Split Fluorescent Protein Triggered by DNA Hybridization |
| URI | https://www.jstor.org/stable/30048079 http://www.pnas.org/content/103/7/2052.abstract https://www.ncbi.nlm.nih.gov/pubmed/16461889 https://www.proquest.com/docview/201381582 https://search.proquest.com/docview/17088935 https://search.proquest.com/docview/67661598 https://pubmed.ncbi.nlm.nih.gov/PMC1413755 |
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