Recombinant human retinoic acid receptor beta. Binding of synthetic retinoids and transcriptional activation
All-trans-retinoic acid mediates cell growth and differentiation by binding to and then activating nuclear retinoid receptor proteins that regulate gene transcription. Recombinant human retinoic acid receptor beta was cloned and expressed in Escherichia coli as a fusion protein rMBP-RAR beta with ma...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-03, Vol.269 (10), p.7297-7303 |
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| container_issue | 10 |
| container_start_page | 7297 |
| container_title | The Journal of biological chemistry |
| container_volume | 269 |
| creator | Lombardo, A Costa, E Chao, W R Toll, L Hobbs, P D Jong, L Lee, M O Pfahl, M Ely, K R Dawson, M I |
| description | All-trans-retinoic acid mediates cell growth and differentiation by binding to and then activating nuclear retinoid receptor
proteins that regulate gene transcription. Recombinant human retinoic acid receptor beta was cloned and expressed in Escherichia
coli as a fusion protein rMBP-RAR beta with maltose-binding protein to facilitate purification. After isolation from bacterial
lysates, rMBP-RAR beta was used for binding with selected retinoids. Scatchard analysis with [11,12-3H2]all-trans-retinoic
acid gave a Kd of 0.34 nM. Competitive binding studies with a series of conformationally restricted aromatic retinoids indicated
that the Ki values for binding to rMBP-RAR beta correlated with the logs of the EC50 values for gene transcriptional activation
(p < or = 0.05) and with those for the relative activation compared to that of all-trans-retinoic acid (p < or = 0.01). Inspection
of binding-activation correlation diagrams indicates candidate structures for improved retinoid agonists or antagonists. |
| doi_str_mv | 10.1016/S0021-9258(17)37283-6 |
| format | Article |
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proteins that regulate gene transcription. Recombinant human retinoic acid receptor beta was cloned and expressed in Escherichia
coli as a fusion protein rMBP-RAR beta with maltose-binding protein to facilitate purification. After isolation from bacterial
lysates, rMBP-RAR beta was used for binding with selected retinoids. Scatchard analysis with [11,12-3H2]all-trans-retinoic
acid gave a Kd of 0.34 nM. Competitive binding studies with a series of conformationally restricted aromatic retinoids indicated
that the Ki values for binding to rMBP-RAR beta correlated with the logs of the EC50 values for gene transcriptional activation
(p < or = 0.05) and with those for the relative activation compared to that of all-trans-retinoic acid (p < or = 0.01). Inspection
of binding-activation correlation diagrams indicates candidate structures for improved retinoid agonists or antagonists.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)37283-6</identifier><identifier>PMID: 8125944</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Binding, Competitive ; Biological and medical sciences ; Cell receptors ; Cell structures and functions ; Cloning, Molecular ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Humans ; Miscellaneous ; Molecular and cellular biology ; Molecular Sequence Data ; Receptors, Retinoic Acid - genetics ; Receptors, Retinoic Acid - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Retinoids - metabolism ; Transcriptional Activation</subject><ispartof>The Journal of biological chemistry, 1994-03, Vol.269 (10), p.7297-7303</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-40cd71461d6b07f1b751e31867f22d914744c613f19fa131c6bd0b697d7cd4a93</citedby><cites>FETCH-LOGICAL-c439t-40cd71461d6b07f1b751e31867f22d914744c613f19fa131c6bd0b697d7cd4a93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4015183$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8125944$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lombardo, A</creatorcontrib><creatorcontrib>Costa, E</creatorcontrib><creatorcontrib>Chao, W R</creatorcontrib><creatorcontrib>Toll, L</creatorcontrib><creatorcontrib>Hobbs, P D</creatorcontrib><creatorcontrib>Jong, L</creatorcontrib><creatorcontrib>Lee, M O</creatorcontrib><creatorcontrib>Pfahl, M</creatorcontrib><creatorcontrib>Ely, K R</creatorcontrib><creatorcontrib>Dawson, M I</creatorcontrib><title>Recombinant human retinoic acid receptor beta. Binding of synthetic retinoids and transcriptional activation</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>All-trans-retinoic acid mediates cell growth and differentiation by binding to and then activating nuclear retinoid receptor
proteins that regulate gene transcription. Recombinant human retinoic acid receptor beta was cloned and expressed in Escherichia
coli as a fusion protein rMBP-RAR beta with maltose-binding protein to facilitate purification. After isolation from bacterial
lysates, rMBP-RAR beta was used for binding with selected retinoids. Scatchard analysis with [11,12-3H2]all-trans-retinoic
acid gave a Kd of 0.34 nM. Competitive binding studies with a series of conformationally restricted aromatic retinoids indicated
that the Ki values for binding to rMBP-RAR beta correlated with the logs of the EC50 values for gene transcriptional activation
(p < or = 0.05) and with those for the relative activation compared to that of all-trans-retinoic acid (p < or = 0.01). Inspection
of binding-activation correlation diagrams indicates candidate structures for improved retinoid agonists or antagonists.</description><subject>Amino Acid Sequence</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Cloning, Molecular</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Miscellaneous</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Receptors, Retinoic Acid - genetics</subject><subject>Receptors, Retinoic Acid - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Retinoids - metabolism</subject><subject>Transcriptional Activation</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV9rHCEUxaUkpNskHyEgJJT2YRLv6Oj4mIb-CQQKSQt5E0edjGVGN-q25Nt3Jrvd1_qil_u798g5CJ0BuQQC_OqBkBoqWTftBxAfqahbWvE3aAVkftAGHg_Qao-8Re9y_kXmwyQcoaMW6kYytkLjvTNx6nzQoeBhM-mAkys-RG-wNt7OlXHrEhPuXNGX-JMP1ocnHHucX0IZZtb8m7AZ62BxSTpkk_y6-Bj0OK8p_rdeihN02Osxu9PdfYx-fvn84-Zbdff96-3N9V1lGJWlYsRYAYyD5R0RPXSiAUeh5aKvayuBCcYMB9qD7DVQMLyzpONSWGEs05Ieo_fbvesUnzcuFzX5bNw46uDiJivBqSQN5_8FgbcgGNAZbLagSTHn5Hq1Tn7S6UUBUUsc6jUOtXitQKjXONQicLYT2HSTs_upnf9z_2LX19nosZ-tMz7vMUaggXaRP99ig38a_vjkVOejGdykai6XL4haCvoXPa6fEA</recordid><startdate>19940311</startdate><enddate>19940311</enddate><creator>Lombardo, A</creator><creator>Costa, E</creator><creator>Chao, W R</creator><creator>Toll, L</creator><creator>Hobbs, P D</creator><creator>Jong, L</creator><creator>Lee, M O</creator><creator>Pfahl, M</creator><creator>Ely, K R</creator><creator>Dawson, M I</creator><general>American Society for Biochemistry and Molecular Biology</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19940311</creationdate><title>Recombinant human retinoic acid receptor beta. Binding of synthetic retinoids and transcriptional activation</title><author>Lombardo, A ; Costa, E ; Chao, W R ; Toll, L ; Hobbs, P D ; Jong, L ; Lee, M O ; Pfahl, M ; Ely, K R ; Dawson, M I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-40cd71461d6b07f1b751e31867f22d914744c613f19fa131c6bd0b697d7cd4a93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Cloning, Molecular</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Miscellaneous</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Receptors, Retinoic Acid - genetics</topic><topic>Receptors, Retinoic Acid - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Retinoids - metabolism</topic><topic>Transcriptional Activation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lombardo, A</creatorcontrib><creatorcontrib>Costa, E</creatorcontrib><creatorcontrib>Chao, W R</creatorcontrib><creatorcontrib>Toll, L</creatorcontrib><creatorcontrib>Hobbs, P D</creatorcontrib><creatorcontrib>Jong, L</creatorcontrib><creatorcontrib>Lee, M O</creatorcontrib><creatorcontrib>Pfahl, M</creatorcontrib><creatorcontrib>Ely, K R</creatorcontrib><creatorcontrib>Dawson, M I</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lombardo, A</au><au>Costa, E</au><au>Chao, W R</au><au>Toll, L</au><au>Hobbs, P D</au><au>Jong, L</au><au>Lee, M O</au><au>Pfahl, M</au><au>Ely, K R</au><au>Dawson, M I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recombinant human retinoic acid receptor beta. Binding of synthetic retinoids and transcriptional activation</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-03-11</date><risdate>1994</risdate><volume>269</volume><issue>10</issue><spage>7297</spage><epage>7303</epage><pages>7297-7303</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>All-trans-retinoic acid mediates cell growth and differentiation by binding to and then activating nuclear retinoid receptor
proteins that regulate gene transcription. Recombinant human retinoic acid receptor beta was cloned and expressed in Escherichia
coli as a fusion protein rMBP-RAR beta with maltose-binding protein to facilitate purification. After isolation from bacterial
lysates, rMBP-RAR beta was used for binding with selected retinoids. Scatchard analysis with [11,12-3H2]all-trans-retinoic
acid gave a Kd of 0.34 nM. Competitive binding studies with a series of conformationally restricted aromatic retinoids indicated
that the Ki values for binding to rMBP-RAR beta correlated with the logs of the EC50 values for gene transcriptional activation
(p < or = 0.05) and with those for the relative activation compared to that of all-trans-retinoic acid (p < or = 0.01). Inspection
of binding-activation correlation diagrams indicates candidate structures for improved retinoid agonists or antagonists.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8125944</pmid><doi>10.1016/S0021-9258(17)37283-6</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1994-03, Vol.269 (10), p.7297-7303 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76390566 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Binding, Competitive Biological and medical sciences Cell receptors Cell structures and functions Cloning, Molecular Escherichia coli Fundamental and applied biological sciences. Psychology Humans Miscellaneous Molecular and cellular biology Molecular Sequence Data Receptors, Retinoic Acid - genetics Receptors, Retinoic Acid - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Retinoids - metabolism Transcriptional Activation |
| title | Recombinant human retinoic acid receptor beta. Binding of synthetic retinoids and transcriptional activation |
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