Aequorin variants with improved bioluminescence properties
The photoprotein aequorin has been widely used as a bioluminescent label in immunoassays, for the determination of calcium concentrations in vivo, and as a reporter in cellular imaging. It is composed of apoaequorin (189 amino acid residues), the imidazopyrazine chromophore coelenterazine and molecu...
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| Veröffentlicht in: | Protein engineering, design and selection design and selection, 2009-04, Vol.22 (4), p.243-248 |
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| creator | Dikici, E. Qu, X. Rowe, L. Millner, L. Logue, C. Deo, S.K. Ensor, M. Daunert, S. |
| description | The photoprotein aequorin has been widely used as a bioluminescent label in immunoassays, for the determination of calcium concentrations in vivo, and as a reporter in cellular imaging. It is composed of apoaequorin (189 amino acid residues), the imidazopyrazine chromophore coelenterazine and molecular oxygen. The emission characteristics of aequorin can be changed by rational design of the protein to introduce mutations in its structure, as well as by substituting different coelenterazine analogues to yield semi-synthetic aequorins. Variants of aequorin were created by mutating residues His16, Met19, Tyr82, Trp86, Trp108, Phe113 and Tyr132. Forty-two aequorin mutants were prepared and combined with 10 different coelenterazine analogues in a search for proteins with different emission wavelengths, altered decay kinetics and improved stability. This spectral tuning strategy resulted in semi-synthetic photoprotein mutants with significantly altered bioluminescent properties. |
| doi_str_mv | 10.1093/protein/gzn083 |
| format | Article |
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It is composed of apoaequorin (189 amino acid residues), the imidazopyrazine chromophore coelenterazine and molecular oxygen. The emission characteristics of aequorin can be changed by rational design of the protein to introduce mutations in its structure, as well as by substituting different coelenterazine analogues to yield semi-synthetic aequorins. Variants of aequorin were created by mutating residues His16, Met19, Tyr82, Trp86, Trp108, Phe113 and Tyr132. Forty-two aequorin mutants were prepared and combined with 10 different coelenterazine analogues in a search for proteins with different emission wavelengths, altered decay kinetics and improved stability. This spectral tuning strategy resulted in semi-synthetic photoprotein mutants with significantly altered bioluminescent properties.</description><identifier>ISSN: 1741-0126</identifier><identifier>EISSN: 1741-0134</identifier><identifier>DOI: 10.1093/protein/gzn083</identifier><identifier>PMID: 19168563</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>aequorin ; Aequorin - chemistry ; Aequorin - genetics ; Aequorin - metabolism ; Apoproteins - chemistry ; Apoproteins - genetics ; Apoproteins - metabolism ; Bacillus - genetics ; bioluminescence ; coelenterazine analogues ; emission wavelength ; Escherichia coli - genetics ; Imidazoles - chemistry ; Imidazoles - metabolism ; Luminescent Agents - chemistry ; Luminescent Agents - metabolism ; Luminescent Proteins - chemistry ; Luminescent Proteins - genetics ; Luminescent Proteins - metabolism ; mutagenesis ; Mutagenesis, Site-Directed ; Mutation ; Original ; Oxygen - metabolism ; Protein Stability ; Pyrazines - chemistry ; Pyrazines - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism</subject><ispartof>Protein engineering, design and selection, 2009-04, Vol.22 (4), p.243-248</ispartof><rights>The Author 2009. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org 2009</rights><rights>The Author 2009. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c518t-8c5dd03f4baa25c5bbd4832bd6276bcd6d5628287d21f2df2a49862d4b0bda173</citedby><cites>FETCH-LOGICAL-c518t-8c5dd03f4baa25c5bbd4832bd6276bcd6d5628287d21f2df2a49862d4b0bda173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,1578,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19168563$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dikici, E.</creatorcontrib><creatorcontrib>Qu, X.</creatorcontrib><creatorcontrib>Rowe, L.</creatorcontrib><creatorcontrib>Millner, L.</creatorcontrib><creatorcontrib>Logue, C.</creatorcontrib><creatorcontrib>Deo, S.K.</creatorcontrib><creatorcontrib>Ensor, M.</creatorcontrib><creatorcontrib>Daunert, S.</creatorcontrib><title>Aequorin variants with improved bioluminescence properties</title><title>Protein engineering, design and selection</title><addtitle>Protein Eng Des Sel</addtitle><description>The photoprotein aequorin has been widely used as a bioluminescent label in immunoassays, for the determination of calcium concentrations in vivo, and as a reporter in cellular imaging. It is composed of apoaequorin (189 amino acid residues), the imidazopyrazine chromophore coelenterazine and molecular oxygen. The emission characteristics of aequorin can be changed by rational design of the protein to introduce mutations in its structure, as well as by substituting different coelenterazine analogues to yield semi-synthetic aequorins. Variants of aequorin were created by mutating residues His16, Met19, Tyr82, Trp86, Trp108, Phe113 and Tyr132. Forty-two aequorin mutants were prepared and combined with 10 different coelenterazine analogues in a search for proteins with different emission wavelengths, altered decay kinetics and improved stability. This spectral tuning strategy resulted in semi-synthetic photoprotein mutants with significantly altered bioluminescent properties.</description><subject>aequorin</subject><subject>Aequorin - chemistry</subject><subject>Aequorin - genetics</subject><subject>Aequorin - metabolism</subject><subject>Apoproteins - chemistry</subject><subject>Apoproteins - genetics</subject><subject>Apoproteins - metabolism</subject><subject>Bacillus - genetics</subject><subject>bioluminescence</subject><subject>coelenterazine analogues</subject><subject>emission wavelength</subject><subject>Escherichia coli - genetics</subject><subject>Imidazoles - chemistry</subject><subject>Imidazoles - metabolism</subject><subject>Luminescent Agents - chemistry</subject><subject>Luminescent Agents - metabolism</subject><subject>Luminescent Proteins - chemistry</subject><subject>Luminescent Proteins - genetics</subject><subject>Luminescent Proteins - metabolism</subject><subject>mutagenesis</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Original</subject><subject>Oxygen - metabolism</subject><subject>Protein Stability</subject><subject>Pyrazines - chemistry</subject><subject>Pyrazines - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><issn>1741-0126</issn><issn>1741-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAURi0EoqWwZYkiFkhdpLWvY8dhUamawgxSJTYFVWwsO3Zal8RO7WR4_HpcZTQ8Nqxs-R4ffVcfQi8JPiG4oadjDJN1_vTmp8eCPkKHpK5IiQmtHu_vwA_Qs5TuMAZeE_IUHZCGcME4PURvz-39HKLzxVZFp_yUim9uui3ckM1bawrtQj8PztvUWt_aIj-PNk7OpufoSaf6ZF_sziP06f27q9WmvPy4_rA6vyxbRsRUipYZg2lXaaWAtUxrUwkK2nCouW4NN4yDAFEbIB2YDlTVCA6m0lgbRWp6hM4W7zjrwZocY4qql2N0g4o_ZFBO_j3x7lbehK0EzhqMeRa82QliuJ9tmuTg8jZ9r7wNc5KABTSEQgZf_wPehTn6vJwEYJV48GXoZIHaGFKKttsnIVg-dCJ3ncilk_zh1Z_5f-O7EjJwvABhHv8vKxfWpcl-39MqfpW8pjWTm-sv8vqCbNZX689yRX8BVHGqFg</recordid><startdate>20090401</startdate><enddate>20090401</enddate><creator>Dikici, E.</creator><creator>Qu, X.</creator><creator>Rowe, L.</creator><creator>Millner, L.</creator><creator>Logue, C.</creator><creator>Deo, S.K.</creator><creator>Ensor, M.</creator><creator>Daunert, S.</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>BSCLL</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>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>5PM</scope></search><sort><creationdate>20090401</creationdate><title>Aequorin variants with improved bioluminescence properties</title><author>Dikici, E. ; Qu, X. ; Rowe, L. ; Millner, L. ; Logue, C. ; Deo, S.K. ; Ensor, M. ; Daunert, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c518t-8c5dd03f4baa25c5bbd4832bd6276bcd6d5628287d21f2df2a49862d4b0bda173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>aequorin</topic><topic>Aequorin - chemistry</topic><topic>Aequorin - genetics</topic><topic>Aequorin - metabolism</topic><topic>Apoproteins - chemistry</topic><topic>Apoproteins - genetics</topic><topic>Apoproteins - metabolism</topic><topic>Bacillus - genetics</topic><topic>bioluminescence</topic><topic>coelenterazine analogues</topic><topic>emission wavelength</topic><topic>Escherichia coli - genetics</topic><topic>Imidazoles - chemistry</topic><topic>Imidazoles - metabolism</topic><topic>Luminescent Agents - chemistry</topic><topic>Luminescent Agents - metabolism</topic><topic>Luminescent Proteins - chemistry</topic><topic>Luminescent Proteins - genetics</topic><topic>Luminescent Proteins - metabolism</topic><topic>mutagenesis</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Original</topic><topic>Oxygen - metabolism</topic><topic>Protein Stability</topic><topic>Pyrazines - chemistry</topic><topic>Pyrazines - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dikici, E.</creatorcontrib><creatorcontrib>Qu, X.</creatorcontrib><creatorcontrib>Rowe, L.</creatorcontrib><creatorcontrib>Millner, L.</creatorcontrib><creatorcontrib>Logue, C.</creatorcontrib><creatorcontrib>Deo, S.K.</creatorcontrib><creatorcontrib>Ensor, M.</creatorcontrib><creatorcontrib>Daunert, S.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein engineering, design and selection</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dikici, E.</au><au>Qu, X.</au><au>Rowe, L.</au><au>Millner, L.</au><au>Logue, C.</au><au>Deo, S.K.</au><au>Ensor, M.</au><au>Daunert, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aequorin variants with improved bioluminescence properties</atitle><jtitle>Protein engineering, design and selection</jtitle><addtitle>Protein Eng Des Sel</addtitle><date>2009-04-01</date><risdate>2009</risdate><volume>22</volume><issue>4</issue><spage>243</spage><epage>248</epage><pages>243-248</pages><issn>1741-0126</issn><eissn>1741-0134</eissn><abstract>The photoprotein aequorin has been widely used as a bioluminescent label in immunoassays, for the determination of calcium concentrations in vivo, and as a reporter in cellular imaging. It is composed of apoaequorin (189 amino acid residues), the imidazopyrazine chromophore coelenterazine and molecular oxygen. The emission characteristics of aequorin can be changed by rational design of the protein to introduce mutations in its structure, as well as by substituting different coelenterazine analogues to yield semi-synthetic aequorins. Variants of aequorin were created by mutating residues His16, Met19, Tyr82, Trp86, Trp108, Phe113 and Tyr132. Forty-two aequorin mutants were prepared and combined with 10 different coelenterazine analogues in a search for proteins with different emission wavelengths, altered decay kinetics and improved stability. This spectral tuning strategy resulted in semi-synthetic photoprotein mutants with significantly altered bioluminescent properties.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>19168563</pmid><doi>10.1093/protein/gzn083</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | aequorin Aequorin - chemistry Aequorin - genetics Aequorin - metabolism Apoproteins - chemistry Apoproteins - genetics Apoproteins - metabolism Bacillus - genetics bioluminescence coelenterazine analogues emission wavelength Escherichia coli - genetics Imidazoles - chemistry Imidazoles - metabolism Luminescent Agents - chemistry Luminescent Agents - metabolism Luminescent Proteins - chemistry Luminescent Proteins - genetics Luminescent Proteins - metabolism mutagenesis Mutagenesis, Site-Directed Mutation Original Oxygen - metabolism Protein Stability Pyrazines - chemistry Pyrazines - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism |
| title | Aequorin variants with improved bioluminescence properties |
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