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Altered DNA binding specificity of Arnt by selection of partner bHLH–PAS proteins
The Ah receptor (AhR) and HLF are transcription factors involved in xenobiotic metabolism and hypoxic response, respectively. AhR and HLF heterodimerize with Arnt as the common partner, and bind to asymmetric E‐boxes termed XRE and HRE, respectively. In order to investigate nucleotide preference of...
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Published in: | Nucleic acids research 2004, Vol.32 (10), p.3169-3179 |
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description | The Ah receptor (AhR) and HLF are transcription factors involved in xenobiotic metabolism and hypoxic response, respectively. AhR and HLF heterodimerize with Arnt as the common partner, and bind to asymmetric E‐boxes termed XRE and HRE, respectively. In order to investigate nucleotide preference of the heterodimers, reporter plasmids with oligonucleotides for XREs or HREs with systematic mutations were constructed and their activity was determined. Comparison of the activity revealed that DNA length and nucleotide preference recognized by Arnt subunit in the two heterodimers were largely different between XRE and HRE. We expressed AhR–Arnt and HLF–Arnt in Escherichia coli and used them for DNA binding. The dissociation constant of HLF–Arnt–HRE was 10.4 ± 1.6 nM. Competition activity of mutated XREs or HREs with wild type was consistent with their transcription activity. Bending of XRE and HRE induced by binding of the relevant heterodimers was observed with stronger bending of XRE than of HRE. By deletional and mutational analyses, an alanine and three arginine (Ala 8, Arg 9, Arg 11 and Arg 12) residues in the basic sequence of HLF were found to be indispensable for the transcriptional activity. |
doi_str_mv | 10.1093/nar/gkh637 |
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AhR and HLF heterodimerize with Arnt as the common partner, and bind to asymmetric E‐boxes termed XRE and HRE, respectively. In order to investigate nucleotide preference of the heterodimers, reporter plasmids with oligonucleotides for XREs or HREs with systematic mutations were constructed and their activity was determined. Comparison of the activity revealed that DNA length and nucleotide preference recognized by Arnt subunit in the two heterodimers were largely different between XRE and HRE. We expressed AhR–Arnt and HLF–Arnt in Escherichia coli and used them for DNA binding. The dissociation constant of HLF–Arnt–HRE was 10.4 ± 1.6 nM. Competition activity of mutated XREs or HREs with wild type was consistent with their transcription activity. Bending of XRE and HRE induced by binding of the relevant heterodimers was observed with stronger bending of XRE than of HRE. By deletional and mutational analyses, an alanine and three arginine (Ala 8, Arg 9, Arg 11 and Arg 12) residues in the basic sequence of HLF were found to be indispensable for the transcriptional activity.</description><identifier>ISSN: 0305-1048</identifier><identifier>ISSN: 1362-4962</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/gkh637</identifier><identifier>PMID: 15190133</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acid Sequence ; Animals ; Aryl Hydrocarbon Receptor Nuclear Translocator ; Basic Helix-Loop-Helix Transcription Factors ; Binding, Competitive ; Cell Line, Tumor ; Dimerization ; DNA - genetics ; DNA - metabolism ; DNA Footprinting ; DNA-Binding Proteins ; Electrophoretic Mobility Shift Assay ; Escherichia coli ; Helix-Loop-Helix Motifs ; Humans ; Mice ; Mutation - genetics ; Protein Binding ; Receptors, Aryl Hydrocarbon - genetics ; Receptors, Aryl Hydrocarbon - metabolism ; Response Elements - genetics ; Substrate Specificity ; Trans-Activators - chemistry ; Trans-Activators - genetics ; Trans-Activators - metabolism ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Transcription, Genetic - genetics</subject><ispartof>Nucleic acids research, 2004, Vol.32 (10), p.3169-3179</ispartof><rights>Copyright Oxford University Press(England) Jun 15, 2004</rights><rights>Copyright © 2004 Oxford University Press 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c566t-a7798dd9f101bb322cf47387a6946bccfa0d51431c64e89764722c73ca86236b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC434443/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC434443/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,4024,27923,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15190133$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kinoshita, Koshi</creatorcontrib><creatorcontrib>Kikuchi, Yasuo</creatorcontrib><creatorcontrib>Sasakura, Yukie</creatorcontrib><creatorcontrib>Suzuki, Masashi</creatorcontrib><creatorcontrib>Fujii‐Kuriyama, Yoshiaki</creatorcontrib><creatorcontrib>Sogawa, Kazuhiro</creatorcontrib><title>Altered DNA binding specificity of Arnt by selection of partner bHLH–PAS proteins</title><title>Nucleic acids research</title><addtitle>Nucl. Acids Res</addtitle><description>The Ah receptor (AhR) and HLF are transcription factors involved in xenobiotic metabolism and hypoxic response, respectively. AhR and HLF heterodimerize with Arnt as the common partner, and bind to asymmetric E‐boxes termed XRE and HRE, respectively. In order to investigate nucleotide preference of the heterodimers, reporter plasmids with oligonucleotides for XREs or HREs with systematic mutations were constructed and their activity was determined. Comparison of the activity revealed that DNA length and nucleotide preference recognized by Arnt subunit in the two heterodimers were largely different between XRE and HRE. We expressed AhR–Arnt and HLF–Arnt in Escherichia coli and used them for DNA binding. The dissociation constant of HLF–Arnt–HRE was 10.4 ± 1.6 nM. Competition activity of mutated XREs or HREs with wild type was consistent with their transcription activity. Bending of XRE and HRE induced by binding of the relevant heterodimers was observed with stronger bending of XRE than of HRE. By deletional and mutational analyses, an alanine and three arginine (Ala 8, Arg 9, Arg 11 and Arg 12) residues in the basic sequence of HLF were found to be indispensable for the transcriptional activity.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Aryl Hydrocarbon Receptor Nuclear Translocator</subject><subject>Basic Helix-Loop-Helix Transcription Factors</subject><subject>Binding, Competitive</subject><subject>Cell Line, Tumor</subject><subject>Dimerization</subject><subject>DNA - genetics</subject><subject>DNA - metabolism</subject><subject>DNA Footprinting</subject><subject>DNA-Binding Proteins</subject><subject>Electrophoretic Mobility Shift Assay</subject><subject>Escherichia coli</subject><subject>Helix-Loop-Helix Motifs</subject><subject>Humans</subject><subject>Mice</subject><subject>Mutation - genetics</subject><subject>Protein Binding</subject><subject>Receptors, Aryl Hydrocarbon - genetics</subject><subject>Receptors, Aryl Hydrocarbon - metabolism</subject><subject>Response Elements - genetics</subject><subject>Substrate Specificity</subject><subject>Trans-Activators - chemistry</subject><subject>Trans-Activators - genetics</subject><subject>Trans-Activators - metabolism</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic - genetics</subject><issn>0305-1048</issn><issn>1362-4962</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqF0c9OFDEcB_CGaGRBLzyAaTx4IBlpp512evAwQWE1GyVBCeHSdDqdpTDbjm2XsDffwTf0SexmN4heODXp7_Prn98XgAOM3mEkyJFT4Wh-e80I3wETTFhZUMHKZ2CCCKoKjGi9C_ZivEEIU1zRF2AXV1ggTMgEnDdDMsF08MOXBrbWddbNYRyNtr3VNq2g72ETXILtCkYzGJ2sd-vNUYXkTIDtdDb9_fPXWXMOx-CTsS6-BM97NUTzarvug-8nH78dT4vZ19NPx82s0BVjqVCci7rrRI8RbltSlrqnnNRcMUFZq3WvUFdhSrBm1NSCM8qz4USrmpWEtWQfvN-cOy7bhem0cSmoQY7BLlRYSa-s_Lfi7LWc-ztJCaWU5P632_7gfyxNTHJhozbDoJzxyyh5iRDDpXgSYiEEZvlRT0PGKs7qDN_8B2_8Mrg8Lbm-lFdlTTM63CAdfIzB9A9fw0iuk5c5eblJPuPXj4fxl26jzqDYABuTuX-oq3ArGSe8ktPLK1lfzC7PLsTnPKI_ay25gA</recordid><startdate>2004</startdate><enddate>2004</enddate><creator>Kinoshita, Koshi</creator><creator>Kikuchi, Yasuo</creator><creator>Sasakura, Yukie</creator><creator>Suzuki, Masashi</creator><creator>Fujii‐Kuriyama, Yoshiaki</creator><creator>Sogawa, Kazuhiro</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>7QR</scope><scope>7SS</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>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>2004</creationdate><title>Altered DNA binding specificity of Arnt by selection of partner bHLH–PAS proteins</title><author>Kinoshita, Koshi ; Kikuchi, Yasuo ; Sasakura, Yukie ; Suzuki, Masashi ; Fujii‐Kuriyama, Yoshiaki ; Sogawa, Kazuhiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c566t-a7798dd9f101bb322cf47387a6946bccfa0d51431c64e89764722c73ca86236b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Aryl Hydrocarbon Receptor Nuclear Translocator</topic><topic>Basic Helix-Loop-Helix Transcription Factors</topic><topic>Binding, Competitive</topic><topic>Cell Line, Tumor</topic><topic>Dimerization</topic><topic>DNA - genetics</topic><topic>DNA - metabolism</topic><topic>DNA Footprinting</topic><topic>DNA-Binding Proteins</topic><topic>Electrophoretic Mobility Shift Assay</topic><topic>Escherichia coli</topic><topic>Helix-Loop-Helix Motifs</topic><topic>Humans</topic><topic>Mice</topic><topic>Mutation - genetics</topic><topic>Protein Binding</topic><topic>Receptors, Aryl Hydrocarbon - genetics</topic><topic>Receptors, Aryl Hydrocarbon - metabolism</topic><topic>Response Elements - genetics</topic><topic>Substrate Specificity</topic><topic>Trans-Activators - chemistry</topic><topic>Trans-Activators - genetics</topic><topic>Trans-Activators - metabolism</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kinoshita, Koshi</creatorcontrib><creatorcontrib>Kikuchi, Yasuo</creatorcontrib><creatorcontrib>Sasakura, Yukie</creatorcontrib><creatorcontrib>Suzuki, Masashi</creatorcontrib><creatorcontrib>Fujii‐Kuriyama, Yoshiaki</creatorcontrib><creatorcontrib>Sogawa, Kazuhiro</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>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</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>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kinoshita, Koshi</au><au>Kikuchi, Yasuo</au><au>Sasakura, Yukie</au><au>Suzuki, Masashi</au><au>Fujii‐Kuriyama, Yoshiaki</au><au>Sogawa, Kazuhiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Altered DNA binding specificity of Arnt by selection of partner bHLH–PAS proteins</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucl. Acids Res</addtitle><date>2004</date><risdate>2004</risdate><volume>32</volume><issue>10</issue><spage>3169</spage><epage>3179</epage><pages>3169-3179</pages><issn>0305-1048</issn><issn>1362-4962</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>The Ah receptor (AhR) and HLF are transcription factors involved in xenobiotic metabolism and hypoxic response, respectively. AhR and HLF heterodimerize with Arnt as the common partner, and bind to asymmetric E‐boxes termed XRE and HRE, respectively. In order to investigate nucleotide preference of the heterodimers, reporter plasmids with oligonucleotides for XREs or HREs with systematic mutations were constructed and their activity was determined. Comparison of the activity revealed that DNA length and nucleotide preference recognized by Arnt subunit in the two heterodimers were largely different between XRE and HRE. We expressed AhR–Arnt and HLF–Arnt in Escherichia coli and used them for DNA binding. The dissociation constant of HLF–Arnt–HRE was 10.4 ± 1.6 nM. Competition activity of mutated XREs or HREs with wild type was consistent with their transcription activity. Bending of XRE and HRE induced by binding of the relevant heterodimers was observed with stronger bending of XRE than of HRE. By deletional and mutational analyses, an alanine and three arginine (Ala 8, Arg 9, Arg 11 and Arg 12) residues in the basic sequence of HLF were found to be indispensable for the transcriptional activity.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>15190133</pmid><doi>10.1093/nar/gkh637</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Aryl Hydrocarbon Receptor Nuclear Translocator Basic Helix-Loop-Helix Transcription Factors Binding, Competitive Cell Line, Tumor Dimerization DNA - genetics DNA - metabolism DNA Footprinting DNA-Binding Proteins Electrophoretic Mobility Shift Assay Escherichia coli Helix-Loop-Helix Motifs Humans Mice Mutation - genetics Protein Binding Receptors, Aryl Hydrocarbon - genetics Receptors, Aryl Hydrocarbon - metabolism Response Elements - genetics Substrate Specificity Trans-Activators - chemistry Trans-Activators - genetics Trans-Activators - metabolism Transcription Factors - genetics Transcription Factors - metabolism Transcription, Genetic - genetics |
title | Altered DNA binding specificity of Arnt by selection of partner bHLH–PAS proteins |
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