A monovalent streptavidin with a single femtomolar biotin binding site
Streptavidin and avidin are used ubiquitously because of the remarkable affinity of their biotin binding, but they are tetramers, which disrupts many of their applications. Making either protein monomeric reduces affinity by at least 10 4 -fold because part of the binding site comes from a neighbori...
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| Veröffentlicht in: | Nature methods 2006-04, Vol.3 (4), p.267-273 |
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| creator | Ting, Alice Y Howarth, Mark Chinnapen, Daniel J-F Gerrow, Kimberly Dorrestein, Pieter C Grandy, Melanie R Kelleher, Neil L El-Husseini, Alaa |
| description | Streptavidin and avidin are used ubiquitously because of the remarkable affinity of their biotin binding, but they are tetramers, which disrupts many of their applications. Making either protein monomeric reduces affinity by at least 10
4
-fold because part of the binding site comes from a neighboring subunit. Here we engineered a streptavidin tetramer with only one functional biotin binding subunit that retained the affinity, off rate and thermostability of wild-type streptavidin. In denaturant, we mixed a streptavidin variant containing three mutations that block biotin binding with wild-type streptavidin in a 3:1 ratio. Then we generated monovalent streptavidin by refolding and nickel-affinity purification. Similarly, we purified defined tetramers with two or three biotin binding subunits. Labeling of site-specifically biotinylated neuroligin-1 with monovalent streptavidin allowed stable neuroligin-1 tracking without cross-linking, whereas wild-type streptavidin aggregated neuroligin-1 and disrupted presynaptic contacts. Monovalent streptavidin should find general application in biomolecule labeling, single-particle tracking and nanotechnology. |
| doi_str_mv | 10.1038/nmeth861 |
| format | Article |
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-fold because part of the binding site comes from a neighboring subunit. Here we engineered a streptavidin tetramer with only one functional biotin binding subunit that retained the affinity, off rate and thermostability of wild-type streptavidin. In denaturant, we mixed a streptavidin variant containing three mutations that block biotin binding with wild-type streptavidin in a 3:1 ratio. Then we generated monovalent streptavidin by refolding and nickel-affinity purification. Similarly, we purified defined tetramers with two or three biotin binding subunits. Labeling of site-specifically biotinylated neuroligin-1 with monovalent streptavidin allowed stable neuroligin-1 tracking without cross-linking, whereas wild-type streptavidin aggregated neuroligin-1 and disrupted presynaptic contacts. Monovalent streptavidin should find general application in biomolecule labeling, single-particle tracking and nanotechnology.</description><identifier>ISSN: 1548-7091</identifier><identifier>EISSN: 1548-7105</identifier><identifier>DOI: 10.1038/nmeth861</identifier><identifier>PMID: 16554831</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Animals ; Binding Sites ; Bioinformatics ; Biological Microscopy ; Biological Techniques ; Biomedical and Life Sciences ; Biomedical Engineering/Biotechnology ; Biotin ; Biotin - chemistry ; Biotin - metabolism ; Biotinylation ; Cell Adhesion Molecules, Neuronal ; Cross-Linking Reagents - pharmacology ; Hippocampus - cytology ; Hippocampus - ultrastructure ; Hybridization ; Kinetics ; Life Sciences ; Membrane Proteins - metabolism ; Molecular probes ; Mutagenesis, Site-Directed ; Mutation ; Nanotechnology ; Nanotechnology - methods ; Nerve Tissue Proteins - metabolism ; Neurons - metabolism ; Nickel ; Physiological aspects ; Protein Denaturation ; Protein Engineering - methods ; Protein Folding ; Proteins ; Proteomics ; Streptavidin - chemistry ; Streptavidin - metabolism ; Synapses - metabolism ; Temperature ; Vitamin B</subject><ispartof>Nature methods, 2006-04, Vol.3 (4), p.267-273</ispartof><rights>Springer Nature America, Inc. 2006</rights><rights>COPYRIGHT 2006 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Apr 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-890c3f52dec76dcdef71ed2bd5846f3edc1eefedee0ca33b695d4be4a5f3a80f3</citedby><cites>FETCH-LOGICAL-c463t-890c3f52dec76dcdef71ed2bd5846f3edc1eefedee0ca33b695d4be4a5f3a80f3</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/nmeth861$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nmeth861$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,2725,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16554831$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ting, Alice Y</creatorcontrib><creatorcontrib>Howarth, Mark</creatorcontrib><creatorcontrib>Chinnapen, Daniel J-F</creatorcontrib><creatorcontrib>Gerrow, Kimberly</creatorcontrib><creatorcontrib>Dorrestein, Pieter C</creatorcontrib><creatorcontrib>Grandy, Melanie R</creatorcontrib><creatorcontrib>Kelleher, Neil L</creatorcontrib><creatorcontrib>El-Husseini, Alaa</creatorcontrib><title>A monovalent streptavidin with a single femtomolar biotin binding site</title><title>Nature methods</title><addtitle>Nat Methods</addtitle><addtitle>Nat Methods</addtitle><description>Streptavidin and avidin are used ubiquitously because of the remarkable affinity of their biotin binding, but they are tetramers, which disrupts many of their applications. Making either protein monomeric reduces affinity by at least 10
4
-fold because part of the binding site comes from a neighboring subunit. Here we engineered a streptavidin tetramer with only one functional biotin binding subunit that retained the affinity, off rate and thermostability of wild-type streptavidin. In denaturant, we mixed a streptavidin variant containing three mutations that block biotin binding with wild-type streptavidin in a 3:1 ratio. Then we generated monovalent streptavidin by refolding and nickel-affinity purification. Similarly, we purified defined tetramers with two or three biotin binding subunits. Labeling of site-specifically biotinylated neuroligin-1 with monovalent streptavidin allowed stable neuroligin-1 tracking without cross-linking, whereas wild-type streptavidin aggregated neuroligin-1 and disrupted presynaptic contacts. Monovalent streptavidin should find general application in biomolecule labeling, single-particle tracking and nanotechnology.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Bioinformatics</subject><subject>Biological Microscopy</subject><subject>Biological Techniques</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedical Engineering/Biotechnology</subject><subject>Biotin</subject><subject>Biotin - chemistry</subject><subject>Biotin - metabolism</subject><subject>Biotinylation</subject><subject>Cell Adhesion Molecules, Neuronal</subject><subject>Cross-Linking Reagents - pharmacology</subject><subject>Hippocampus - cytology</subject><subject>Hippocampus - ultrastructure</subject><subject>Hybridization</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular probes</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Nanotechnology</subject><subject>Nanotechnology - methods</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons - metabolism</subject><subject>Nickel</subject><subject>Physiological aspects</subject><subject>Protein Denaturation</subject><subject>Protein Engineering - methods</subject><subject>Protein Folding</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Streptavidin - chemistry</subject><subject>Streptavidin - metabolism</subject><subject>Synapses - metabolism</subject><subject>Temperature</subject><subject>Vitamin 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Methods</addtitle><date>2006-04-01</date><risdate>2006</risdate><volume>3</volume><issue>4</issue><spage>267</spage><epage>273</epage><pages>267-273</pages><issn>1548-7091</issn><eissn>1548-7105</eissn><abstract>Streptavidin and avidin are used ubiquitously because of the remarkable affinity of their biotin binding, but they are tetramers, which disrupts many of their applications. Making either protein monomeric reduces affinity by at least 10
4
-fold because part of the binding site comes from a neighboring subunit. Here we engineered a streptavidin tetramer with only one functional biotin binding subunit that retained the affinity, off rate and thermostability of wild-type streptavidin. In denaturant, we mixed a streptavidin variant containing three mutations that block biotin binding with wild-type streptavidin in a 3:1 ratio. Then we generated monovalent streptavidin by refolding and nickel-affinity purification. Similarly, we purified defined tetramers with two or three biotin binding subunits. Labeling of site-specifically biotinylated neuroligin-1 with monovalent streptavidin allowed stable neuroligin-1 tracking without cross-linking, whereas wild-type streptavidin aggregated neuroligin-1 and disrupted presynaptic contacts. Monovalent streptavidin should find general application in biomolecule labeling, single-particle tracking and nanotechnology.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>16554831</pmid><doi>10.1038/nmeth861</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Nature methods, 2006-04, Vol.3 (4), p.267-273 |
| issn | 1548-7091 1548-7105 |
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| subjects | Animals Binding Sites Bioinformatics Biological Microscopy Biological Techniques Biomedical and Life Sciences Biomedical Engineering/Biotechnology Biotin Biotin - chemistry Biotin - metabolism Biotinylation Cell Adhesion Molecules, Neuronal Cross-Linking Reagents - pharmacology Hippocampus - cytology Hippocampus - ultrastructure Hybridization Kinetics Life Sciences Membrane Proteins - metabolism Molecular probes Mutagenesis, Site-Directed Mutation Nanotechnology Nanotechnology - methods Nerve Tissue Proteins - metabolism Neurons - metabolism Nickel Physiological aspects Protein Denaturation Protein Engineering - methods Protein Folding Proteins Proteomics Streptavidin - chemistry Streptavidin - metabolism Synapses - metabolism Temperature Vitamin B |
| title | A monovalent streptavidin with a single femtomolar biotin binding site |
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