Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
Fluorescent proteins are genetically encoded, easily imaged reporters crucial in biology and biotechnology 1 , 2 . When a protein is tagged by fusion to a fluorescent protein, interactions between fluorescent proteins can undesirably disturb targeting or function 3 . Unfortunately, all wild-type yel...
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| Veröffentlicht in: | Nature biotechnology 2004-12, Vol.22 (12), p.1567-1572 |
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| creator | Shaner, Nathan C Campbell, Robert E Steinbach, Paul A Giepmans, Ben N G Palmer, Amy E Tsien, Roger Y |
| description | Fluorescent proteins are genetically encoded, easily imaged reporters crucial in biology and biotechnology
1
,
2
. When a protein is tagged by fusion to a fluorescent protein, interactions between fluorescent proteins can undesirably disturb targeting or function
3
. Unfortunately, all wild-type yellow-to-red fluorescent proteins reported so far are obligately tetrameric and often toxic or disruptive
4
,
5
. The first true monomer was mRFP1, derived from the
Discosoma
sp. fluorescent protein “DsRed” by directed evolution first to increase the speed of maturation
6
, then to break each subunit interface while restoring fluorescence, which cumulatively required 33 substitutions
7
. Although mRFP1 has already proven widely useful, several properties could bear improvement and more colors would be welcome. We report the next generation of monomers. The latest red version matures more completely, is more tolerant of N-terminal fusions and is over tenfold more photostable than mRFP1. Three monomers with distinguishable hues from yellow-orange to red-orange have higher quantum efficiencies. |
| doi_str_mv | 10.1038/nbt1037 |
| format | Article |
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1
,
2
. When a protein is tagged by fusion to a fluorescent protein, interactions between fluorescent proteins can undesirably disturb targeting or function
3
. Unfortunately, all wild-type yellow-to-red fluorescent proteins reported so far are obligately tetrameric and often toxic or disruptive
4
,
5
. The first true monomer was mRFP1, derived from the
Discosoma
sp. fluorescent protein “DsRed” by directed evolution first to increase the speed of maturation
6
, then to break each subunit interface while restoring fluorescence, which cumulatively required 33 substitutions
7
. Although mRFP1 has already proven widely useful, several properties could bear improvement and more colors would be welcome. We report the next generation of monomers. The latest red version matures more completely, is more tolerant of N-terminal fusions and is over tenfold more photostable than mRFP1. Three monomers with distinguishable hues from yellow-orange to red-orange have higher quantum efficiencies.</description><identifier>ISSN: 1087-0156</identifier><identifier>EISSN: 1546-1696</identifier><identifier>DOI: 10.1038/nbt1037</identifier><identifier>PMID: 15558047</identifier><identifier>CODEN: NABIF9</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Agriculture ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Anthozoa - genetics ; Anthozoa - metabolism ; Bioinformatics ; Biological and medical sciences ; Biomedical Engineering/Biotechnology ; Biomedicine ; Biotechnology ; Discosoma ; Fluorescence ; Fruits ; Fundamental and applied biological sciences. Psychology ; Genetic Enhancement - methods ; letter ; Life Sciences ; Luminescent Proteins - biosynthesis ; Luminescent Proteins - chemistry ; Luminescent Proteins - genetics ; Methods. Procedures. Technologies ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein engineering ; Protein Engineering - methods ; Proteins ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Red Fluorescent Protein ; Spectrometry, Fluorescence - methods</subject><ispartof>Nature biotechnology, 2004-12, Vol.22 (12), p.1567-1572</ispartof><rights>Springer Nature Limited 2004</rights><rights>2005 INIST-CNRS</rights><rights>COPYRIGHT 2004 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Dec 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c610t-39166af0471d2070bf2bef87d44cf2179f6a4729bc0414be3641c8eee14dfc773</citedby><cites>FETCH-LOGICAL-c610t-39166af0471d2070bf2bef87d44cf2179f6a4729bc0414be3641c8eee14dfc773</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nbt1037$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nbt1037$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16328291$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15558047$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shaner, Nathan C</creatorcontrib><creatorcontrib>Campbell, Robert E</creatorcontrib><creatorcontrib>Steinbach, Paul A</creatorcontrib><creatorcontrib>Giepmans, Ben N G</creatorcontrib><creatorcontrib>Palmer, Amy E</creatorcontrib><creatorcontrib>Tsien, Roger Y</creatorcontrib><title>Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein</title><title>Nature biotechnology</title><addtitle>Nat Biotechnol</addtitle><addtitle>Nat Biotechnol</addtitle><description>Fluorescent proteins are genetically encoded, easily imaged reporters crucial in biology and biotechnology
1
,
2
. When a protein is tagged by fusion to a fluorescent protein, interactions between fluorescent proteins can undesirably disturb targeting or function
3
. Unfortunately, all wild-type yellow-to-red fluorescent proteins reported so far are obligately tetrameric and often toxic or disruptive
4
,
5
. The first true monomer was mRFP1, derived from the
Discosoma
sp. fluorescent protein “DsRed” by directed evolution first to increase the speed of maturation
6
, then to break each subunit interface while restoring fluorescence, which cumulatively required 33 substitutions
7
. Although mRFP1 has already proven widely useful, several properties could bear improvement and more colors would be welcome. We report the next generation of monomers. The latest red version matures more completely, is more tolerant of N-terminal fusions and is over tenfold more photostable than mRFP1. Three monomers with distinguishable hues from yellow-orange to red-orange have higher quantum efficiencies.</description><subject>Agriculture</subject><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution</subject><subject>Animals</subject><subject>Anthozoa - genetics</subject><subject>Anthozoa - metabolism</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biomedical Engineering/Biotechnology</subject><subject>Biomedicine</subject><subject>Biotechnology</subject><subject>Discosoma</subject><subject>Fluorescence</subject><subject>Fruits</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic Enhancement - methods</subject><subject>letter</subject><subject>Life Sciences</subject><subject>Luminescent Proteins - biosynthesis</subject><subject>Luminescent Proteins - chemistry</subject><subject>Luminescent Proteins - genetics</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Protein engineering</subject><subject>Protein Engineering - methods</subject><subject>Proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Red Fluorescent Protein</subject><subject>Spectrometry, Fluorescence - methods</subject><issn>1087-0156</issn><issn>1546-1696</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkluL3CAUx6W0dLfT0m9QpLC9QDPVaDR5XLa3gYWF3l7FmOOQJdFZTdrut-8ZJjDs0ocqeER__3PRQ8hzztacifp9aCe0-gE55ZVUBVeNeoh7VuuC8UqdkCc5XzPGlFTqMTnhVVXVTOpTcrMZdyn-go6OMcQRUu9ogu4djcmGLVAbOnoLwxB_Uz_MMUF2ECaKmgn6kGmHir3apzjSD312McfR0rxb7938S_OUPPJ2yPBssSvy49PH7xdfisurz5uL88vCKc6mQjRcKesxSd6VTLPWly34WndSOl9y3XhlpS6b1jHJZQtCSe5qAOCy805rsSKvDn4x7s0MeTIjpoel2ABxzoZrLSstGwRf3gOv45wC5mZKHI3QQiC0PkBbO4Dpg49Tsg5nB2PvYgDf4_k5b5ioOMN1Rd7eESAzwZ9pa-eczebb1_9nr37eZV8fWJdizgm82aV-tOnWcGb2vWCWXkDyxVLX3I7QHbnl8xE4WwCbnR08_rjr85FToqzLhiP35sBlvMKmSMcHuh_zL0Fvx_k</recordid><startdate>20041201</startdate><enddate>20041201</enddate><creator>Shaner, Nathan C</creator><creator>Campbell, Robert E</creator><creator>Steinbach, Paul A</creator><creator>Giepmans, Ben N G</creator><creator>Palmer, Amy E</creator><creator>Tsien, Roger Y</creator><general>Nature Publishing Group UK</general><general>Nature</general><general>Nature Publishing Group</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>RC3</scope></search><sort><creationdate>20041201</creationdate><title>Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein</title><author>Shaner, Nathan C ; Campbell, Robert E ; Steinbach, Paul A ; Giepmans, Ben N G ; Palmer, Amy E ; Tsien, Roger Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c610t-39166af0471d2070bf2bef87d44cf2179f6a4729bc0414be3641c8eee14dfc773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Agriculture</topic><topic>Amino Acid Sequence</topic><topic>Amino Acid Substitution</topic><topic>Animals</topic><topic>Anthozoa - genetics</topic><topic>Anthozoa - metabolism</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biomedical Engineering/Biotechnology</topic><topic>Biomedicine</topic><topic>Biotechnology</topic><topic>Discosoma</topic><topic>Fluorescence</topic><topic>Fruits</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic Enhancement - methods</topic><topic>letter</topic><topic>Life Sciences</topic><topic>Luminescent Proteins - biosynthesis</topic><topic>Luminescent Proteins - chemistry</topic><topic>Luminescent Proteins - genetics</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Protein engineering</topic><topic>Protein Engineering - methods</topic><topic>Proteins</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Red Fluorescent Protein</topic><topic>Spectrometry, Fluorescence - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shaner, Nathan C</creatorcontrib><creatorcontrib>Campbell, Robert E</creatorcontrib><creatorcontrib>Steinbach, Paul A</creatorcontrib><creatorcontrib>Giepmans, Ben N G</creatorcontrib><creatorcontrib>Palmer, Amy E</creatorcontrib><creatorcontrib>Tsien, Roger Y</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE 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Biotechnol</addtitle><date>2004-12-01</date><risdate>2004</risdate><volume>22</volume><issue>12</issue><spage>1567</spage><epage>1572</epage><pages>1567-1572</pages><issn>1087-0156</issn><eissn>1546-1696</eissn><coden>NABIF9</coden><abstract>Fluorescent proteins are genetically encoded, easily imaged reporters crucial in biology and biotechnology
1
,
2
. When a protein is tagged by fusion to a fluorescent protein, interactions between fluorescent proteins can undesirably disturb targeting or function
3
. Unfortunately, all wild-type yellow-to-red fluorescent proteins reported so far are obligately tetrameric and often toxic or disruptive
4
,
5
. The first true monomer was mRFP1, derived from the
Discosoma
sp. fluorescent protein “DsRed” by directed evolution first to increase the speed of maturation
6
, then to break each subunit interface while restoring fluorescence, which cumulatively required 33 substitutions
7
. Although mRFP1 has already proven widely useful, several properties could bear improvement and more colors would be welcome. We report the next generation of monomers. The latest red version matures more completely, is more tolerant of N-terminal fusions and is over tenfold more photostable than mRFP1. Three monomers with distinguishable hues from yellow-orange to red-orange have higher quantum efficiencies.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>15558047</pmid><doi>10.1038/nbt1037</doi><tpages>6</tpages></addata></record> |
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| ispartof | Nature biotechnology, 2004-12, Vol.22 (12), p.1567-1572 |
| issn | 1087-0156 1546-1696 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals; Nature |
| subjects | Agriculture Amino Acid Sequence Amino Acid Substitution Animals Anthozoa - genetics Anthozoa - metabolism Bioinformatics Biological and medical sciences Biomedical Engineering/Biotechnology Biomedicine Biotechnology Discosoma Fluorescence Fruits Fundamental and applied biological sciences. Psychology Genetic Enhancement - methods letter Life Sciences Luminescent Proteins - biosynthesis Luminescent Proteins - chemistry Luminescent Proteins - genetics Methods. Procedures. Technologies Molecular Sequence Data Mutagenesis, Site-Directed Protein engineering Protein Engineering - methods Proteins Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Red Fluorescent Protein Spectrometry, Fluorescence - methods |
| title | Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein |
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