Combinational Application of Surface Plasmon Resonance Spectroscopy and Quartz Crystal Microbalance for Studying Nuclear Hormone Receptor−Response Element Interactions
Conventional methodologies for studying protein−DNA complexes, such as electrophoretic mobility shift assays (EMSAs), lack the real-time sensitivity and precision to accurately characterize the complex dynamics of interactions between transcription factors and their binding sites. To better understa...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2006-08, Vol.78 (15), p.5552-5558 |
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| creator | Su, Xiaodi Lin, Chin-Yo O'Shea, Sean J Teh, Huey Fang Peh, Wendy Y. X Thomsen, Jane S |
| description | Conventional methodologies for studying protein−DNA complexes, such as electrophoretic mobility shift assays (EMSAs), lack the real-time sensitivity and precision to accurately characterize the complex dynamics of interactions between transcription factors and their binding sites. To better understand the interactions between estrogen receptor (ER) subtypes and the estrogen response elements (EREs), we employed surface plasmon resonance (SPR) spectroscopy and quartz crystal microbalance with dissipation measurement (QCM-D) and made the following observations: (1) base substitutions in ERE half-sites reduced binding affinity for both ERα and ERβ, (2) ERα has a higher sequence specificity than ERβ or there were more nonspecific interactions between ERβ and control DNA, and (3) ERα bound ERE as dimers and ERβ bound as tetramers. These findings highlight intrinsic differences in DNA-binding properties between receptor subtypes, which are not apparent based on the high degree of conservation (96% identity) in their DNA-binding domains and results from EMSA studies. With this study, we demonstrate the potential of utilizing SPR and QCM in combination for a comprehensive characterization of ER−DNA interactions, including sequence-dependent binding mechanisms and structural differences in ERα−DNA and ERβ−DNA complexes. |
| doi_str_mv | 10.1021/ac0606103 |
| format | Article |
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To better understand the interactions between estrogen receptor (ER) subtypes and the estrogen response elements (EREs), we employed surface plasmon resonance (SPR) spectroscopy and quartz crystal microbalance with dissipation measurement (QCM-D) and made the following observations: (1) base substitutions in ERE half-sites reduced binding affinity for both ERα and ERβ, (2) ERα has a higher sequence specificity than ERβ or there were more nonspecific interactions between ERβ and control DNA, and (3) ERα bound ERE as dimers and ERβ bound as tetramers. These findings highlight intrinsic differences in DNA-binding properties between receptor subtypes, which are not apparent based on the high degree of conservation (96% identity) in their DNA-binding domains and results from EMSA studies. 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X</creatorcontrib><creatorcontrib>Thomsen, Jane S</creatorcontrib><title>Combinational Application of Surface Plasmon Resonance Spectroscopy and Quartz Crystal Microbalance for Studying Nuclear Hormone Receptor−Response Element Interactions</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>Conventional methodologies for studying protein−DNA complexes, such as electrophoretic mobility shift assays (EMSAs), lack the real-time sensitivity and precision to accurately characterize the complex dynamics of interactions between transcription factors and their binding sites. To better understand the interactions between estrogen receptor (ER) subtypes and the estrogen response elements (EREs), we employed surface plasmon resonance (SPR) spectroscopy and quartz crystal microbalance with dissipation measurement (QCM-D) and made the following observations: (1) base substitutions in ERE half-sites reduced binding affinity for both ERα and ERβ, (2) ERα has a higher sequence specificity than ERβ or there were more nonspecific interactions between ERβ and control DNA, and (3) ERα bound ERE as dimers and ERβ bound as tetramers. These findings highlight intrinsic differences in DNA-binding properties between receptor subtypes, which are not apparent based on the high degree of conservation (96% identity) in their DNA-binding domains and results from EMSA studies. With this study, we demonstrate the potential of utilizing SPR and QCM in combination for a comprehensive characterization of ER−DNA interactions, including sequence-dependent binding mechanisms and structural differences in ERα−DNA and ERβ−DNA complexes.</description><subject>Analytical chemistry</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biosensors</subject><subject>Chemistry</subject><subject>Crystals</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - analysis</subject><subject>Estrogens</subject><subject>Exact sciences and technology</subject><subject>General, instrumentation</subject><subject>Humans</subject><subject>Potassium Chloride - chemistry</subject><subject>Proteins</subject><subject>Quartz</subject><subject>Real time</subject><subject>Receptors, Estrogen - analysis</subject><subject>Response Elements</subject><subject>Sensitivity and Specificity</subject><subject>Spectrometric and optical methods</subject><subject>Spectrum analysis</subject><subject>Surface Plasmon Resonance</subject><subject>Time Factors</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkcFu1DAQhi0EokvhwAsgCwkkDoGxk9jOsawKW1Gg7Zaz5TgTlJLEqe1ILE_AmbfgtXgS3O6qK8HJ8synTzP_EPKUwWsGnL0xFgQIBvk9smAlh0woxe-TBQDkGZcAB-RRCFcAjAETD8kBE0oqVZUL8nvphrobTezcaHp6NE19Z29_1LV0PfvWWKRnvQlDKl1gSNiYKusJbfQuWDdtqBkbej4bH3_Qpd-EmEQfO-tdbfpbuHWeruPcbLrxK_002x6NpyvnkxKT0-IUnf_z81fST24MSI97HHCM9GSM6I29GSc8Jg9a0wd8snsPyZd3x5fLVXb6-f3J8ug0M4UsYlaV1pRpT95K4KJB1SiBNfCq5YzLpjElqharui5k24gKQJmiKhWUzFZYKp4fkpdb7-Td9Ywh6qELFvu0Cro5aKFEJYs8T-Dzf8ArN_uUYtCcSSVFUVUJerWFUhwheGz15LvB-I1moG-Op--Ol9hnO-FcD9jsyd21EvBiB5hgTd_6lG4X9pwClrOiSFy25boQ8ftd3_hvWshclvrybK3PP7wt16v8Qhd7r7Fhv8T_A_4FFpe_6w</recordid><startdate>20060801</startdate><enddate>20060801</enddate><creator>Su, Xiaodi</creator><creator>Lin, Chin-Yo</creator><creator>O'Shea, Sean J</creator><creator>Teh, Huey Fang</creator><creator>Peh, Wendy Y. 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X</au><au>Thomsen, Jane S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Combinational Application of Surface Plasmon Resonance Spectroscopy and Quartz Crystal Microbalance for Studying Nuclear Hormone Receptor−Response Element Interactions</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>2006-08-01</date><risdate>2006</risdate><volume>78</volume><issue>15</issue><spage>5552</spage><epage>5558</epage><pages>5552-5558</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>Conventional methodologies for studying protein−DNA complexes, such as electrophoretic mobility shift assays (EMSAs), lack the real-time sensitivity and precision to accurately characterize the complex dynamics of interactions between transcription factors and their binding sites. To better understand the interactions between estrogen receptor (ER) subtypes and the estrogen response elements (EREs), we employed surface plasmon resonance (SPR) spectroscopy and quartz crystal microbalance with dissipation measurement (QCM-D) and made the following observations: (1) base substitutions in ERE half-sites reduced binding affinity for both ERα and ERβ, (2) ERα has a higher sequence specificity than ERβ or there were more nonspecific interactions between ERβ and control DNA, and (3) ERα bound ERE as dimers and ERβ bound as tetramers. These findings highlight intrinsic differences in DNA-binding properties between receptor subtypes, which are not apparent based on the high degree of conservation (96% identity) in their DNA-binding domains and results from EMSA studies. With this study, we demonstrate the potential of utilizing SPR and QCM in combination for a comprehensive characterization of ER−DNA interactions, including sequence-dependent binding mechanisms and structural differences in ERα−DNA and ERβ−DNA complexes.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>16878895</pmid><doi>10.1021/ac0606103</doi><tpages>7</tpages></addata></record> |
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| subjects | Analytical chemistry Binding sites Biochemistry Biosensors Chemistry Crystals Deoxyribonucleic acid DNA DNA - analysis Estrogens Exact sciences and technology General, instrumentation Humans Potassium Chloride - chemistry Proteins Quartz Real time Receptors, Estrogen - analysis Response Elements Sensitivity and Specificity Spectrometric and optical methods Spectrum analysis Surface Plasmon Resonance Time Factors |
| title | Combinational Application of Surface Plasmon Resonance Spectroscopy and Quartz Crystal Microbalance for Studying Nuclear Hormone Receptor−Response Element Interactions |
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