A Repressor with Similarities to Prokaryotic and Eukaryotic DNA Helicases Controls the Assembly of the CAAT Box Binding Complex at a Photosynthesis Gene Promoter
A single nucleotide exchange in a promoter region located immediately upstream of the CAAT box of the spinach photosynthesis gene AtpC (gene product is subunit γ of the chloroplast ATP synthase) prevents the formation of a secondary structure and causes an unregulated, constitutive high level of exp...
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creator | Bezhani, Staver Sherameti, Irena Pfannschmidt, Thomas Oelmüller, Ralf |
description | A single nucleotide exchange in a promoter region located immediately upstream of the CAAT box of the spinach photosynthesis gene AtpC (gene product is subunit γ of the chloroplast ATP synthase) prevents the formation of a secondary structure and causes an unregulated, constitutive high level of expression (Kusnetsov, V., Landsberger, M., Oelmüller, R. (1999)J. Biol. Chem. 274, 36009–36014). We have isolated cDNAs for ATPC-2, a new polypeptide with homologies to pro- and eukaryotic helicases, which specifically binds to this promoter region. Binding of ATPC-2 competes strongly with that of a CAAT box binding factor (CBF), consistent with the idea that both complexes cannot be formed simultaneously because of sterical reasons. In gel mobility shift assays, high binding activities of ATPC-2 and low binding activities of CBF were observed with nuclear extracts from tissue with low AtpC expression levels, and the opposite was observed with extracts from tissues with high AtpCexpression levels. Binding of ATPC-2 to the mutant sequence, which directs a constitutively high level expression in vivo and prevents the formation of a secondary structure in vitro,is significantly weaker than binding to the wild-type sequence. Again, the opposite results were obtained for the CBF. Thus, we conclude that the assembly of the CBF·DNA complex stimulates transcription of AtpC and that CBF binding is prevented if ATPC-2 is bound to the promoter region. The novel mechanism of gene regulation and the role of the helicase-like protein ATPC-2 as a potential transcriptional repressor is discussed in relation to its modular structure. |
doi_str_mv | 10.1074/jbc.M010945200 |
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(1999)J. Biol. Chem. 274, 36009–36014). We have isolated cDNAs for ATPC-2, a new polypeptide with homologies to pro- and eukaryotic helicases, which specifically binds to this promoter region. Binding of ATPC-2 competes strongly with that of a CAAT box binding factor (CBF), consistent with the idea that both complexes cannot be formed simultaneously because of sterical reasons. In gel mobility shift assays, high binding activities of ATPC-2 and low binding activities of CBF were observed with nuclear extracts from tissue with low AtpC expression levels, and the opposite was observed with extracts from tissues with high AtpCexpression levels. Binding of ATPC-2 to the mutant sequence, which directs a constitutively high level expression in vivo and prevents the formation of a secondary structure in vitro,is significantly weaker than binding to the wild-type sequence. Again, the opposite results were obtained for the CBF. Thus, we conclude that the assembly of the CBF·DNA complex stimulates transcription of AtpC and that CBF binding is prevented if ATPC-2 is bound to the promoter region. The novel mechanism of gene regulation and the role of the helicase-like protein ATPC-2 as a potential transcriptional repressor is discussed in relation to its modular structure.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M010945200</identifier><identifier>PMID: 11274172</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Arabidopsis - genetics ; ATPC-2 protein ; CCAAT-Binding Factor - metabolism ; Cloning, Molecular ; DNA Helicases - genetics ; DNA Helicases - physiology ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - physiology ; Eukaryotic Cells - metabolism ; Gene Expression Regulation, Plant ; Macromolecular Substances ; Molecular Sequence Data ; Photosynthesis ; Plant Proteins - genetics ; Plant Proteins - physiology ; Prokaryotic Cells - metabolism ; Promoter Regions, Genetic ; Proton-Translocating ATPases - genetics ; Repressor Proteins - genetics ; Repressor Proteins - physiology ; Response Elements ; Sequence Homology, Amino Acid ; Spinacia oleracea</subject><ispartof>The Journal of biological chemistry, 2001-06, Vol.276 (26), p.23785-23789</ispartof><rights>2001 © 2001 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-7b6b408b501ced0ffa056b350fa7245c59b827205f5d1b7b9e37db4511d89f463</citedby><cites>FETCH-LOGICAL-c440t-7b6b408b501ced0ffa056b350fa7245c59b827205f5d1b7b9e37db4511d89f463</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11274172$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bezhani, Staver</creatorcontrib><creatorcontrib>Sherameti, Irena</creatorcontrib><creatorcontrib>Pfannschmidt, Thomas</creatorcontrib><creatorcontrib>Oelmüller, Ralf</creatorcontrib><title>A Repressor with Similarities to Prokaryotic and Eukaryotic DNA Helicases Controls the Assembly of the CAAT Box Binding Complex at a Photosynthesis Gene Promoter</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A single nucleotide exchange in a promoter region located immediately upstream of the CAAT box of the spinach photosynthesis gene AtpC (gene product is subunit γ of the chloroplast ATP synthase) prevents the formation of a secondary structure and causes an unregulated, constitutive high level of expression (Kusnetsov, V., Landsberger, M., Oelmüller, R. (1999)J. Biol. Chem. 274, 36009–36014). We have isolated cDNAs for ATPC-2, a new polypeptide with homologies to pro- and eukaryotic helicases, which specifically binds to this promoter region. Binding of ATPC-2 competes strongly with that of a CAAT box binding factor (CBF), consistent with the idea that both complexes cannot be formed simultaneously because of sterical reasons. In gel mobility shift assays, high binding activities of ATPC-2 and low binding activities of CBF were observed with nuclear extracts from tissue with low AtpC expression levels, and the opposite was observed with extracts from tissues with high AtpCexpression levels. Binding of ATPC-2 to the mutant sequence, which directs a constitutively high level expression in vivo and prevents the formation of a secondary structure in vitro,is significantly weaker than binding to the wild-type sequence. Again, the opposite results were obtained for the CBF. Thus, we conclude that the assembly of the CBF·DNA complex stimulates transcription of AtpC and that CBF binding is prevented if ATPC-2 is bound to the promoter region. The novel mechanism of gene regulation and the role of the helicase-like protein ATPC-2 as a potential transcriptional repressor is discussed in relation to its modular structure.</description><subject>Amino Acid Sequence</subject><subject>Arabidopsis - genetics</subject><subject>ATPC-2 protein</subject><subject>CCAAT-Binding Factor - metabolism</subject><subject>Cloning, Molecular</subject><subject>DNA Helicases - genetics</subject><subject>DNA Helicases - physiology</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - physiology</subject><subject>Eukaryotic Cells - metabolism</subject><subject>Gene Expression Regulation, Plant</subject><subject>Macromolecular Substances</subject><subject>Molecular Sequence Data</subject><subject>Photosynthesis</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - physiology</subject><subject>Prokaryotic Cells - metabolism</subject><subject>Promoter Regions, Genetic</subject><subject>Proton-Translocating ATPases - genetics</subject><subject>Repressor Proteins - genetics</subject><subject>Repressor Proteins - physiology</subject><subject>Response Elements</subject><subject>Sequence Homology, Amino Acid</subject><subject>Spinacia oleracea</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv1DAQhS0EokvhyhH5gLhlsR07To7pUlqkAhUUiZtlO5PGJYm3tpd2fw7_FC-7oifEyNJopO_NWO8h9JKSJSWSv70xdvmRUNJwwQh5hBaU1GVRCvr9MVoQwmjRMFEfoWcx3pBcvKFP0RGlTHIq2QL9avEXWAeI0Qd859KAv7rJjTq45CDi5PFl8D902PrkLNZzh083f8d3n1p8DqOzOmZ25ecU_JhFA-A2RpjMuMW-_zOv2vYKn_h7fOLmzs3XmZ7WI9xjnbDGl4NPPm7nTEYX8RnMsLs7-QThOXrS6zHCi0M_Rt_en16tzouLz2cfVu1FYTknqZCmMpzURhBqoSN9r4moTClIryXjworG1EwyInrRUSNNA6XsDBeUdnXT86o8Rm_2e9fB324gJjW5aGEc9Qx-E5UkjWgY4f8FqawbISqRweUetMHHGKBX6-CmbJ6iRO3SUzk99ZBeFrw6bN6YCboH_BBXBl7vgcFdD3cugDLO2wEmxWSlWH6lrHeH6z0G2a-fDoKK1sGcfckSm1Tn3b--8BsO07Vy</recordid><startdate>20010629</startdate><enddate>20010629</enddate><creator>Bezhani, Staver</creator><creator>Sherameti, Irena</creator><creator>Pfannschmidt, Thomas</creator><creator>Oelmüller, Ralf</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20010629</creationdate><title>A Repressor with Similarities to Prokaryotic and Eukaryotic DNA Helicases Controls the Assembly of the CAAT Box Binding Complex at a Photosynthesis Gene Promoter</title><author>Bezhani, Staver ; Sherameti, Irena ; Pfannschmidt, Thomas ; Oelmüller, Ralf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-7b6b408b501ced0ffa056b350fa7245c59b827205f5d1b7b9e37db4511d89f463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Arabidopsis - genetics</topic><topic>ATPC-2 protein</topic><topic>CCAAT-Binding Factor - metabolism</topic><topic>Cloning, Molecular</topic><topic>DNA Helicases - genetics</topic><topic>DNA Helicases - physiology</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - physiology</topic><topic>Eukaryotic Cells - metabolism</topic><topic>Gene Expression Regulation, Plant</topic><topic>Macromolecular Substances</topic><topic>Molecular Sequence Data</topic><topic>Photosynthesis</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - physiology</topic><topic>Prokaryotic Cells - metabolism</topic><topic>Promoter Regions, Genetic</topic><topic>Proton-Translocating ATPases - genetics</topic><topic>Repressor Proteins - genetics</topic><topic>Repressor Proteins - physiology</topic><topic>Response Elements</topic><topic>Sequence Homology, Amino Acid</topic><topic>Spinacia oleracea</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bezhani, Staver</creatorcontrib><creatorcontrib>Sherameti, Irena</creatorcontrib><creatorcontrib>Pfannschmidt, Thomas</creatorcontrib><creatorcontrib>Oelmüller, Ralf</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics 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>Bezhani, Staver</au><au>Sherameti, Irena</au><au>Pfannschmidt, Thomas</au><au>Oelmüller, Ralf</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Repressor with Similarities to Prokaryotic and Eukaryotic DNA Helicases Controls the Assembly of the CAAT Box Binding Complex at a Photosynthesis Gene Promoter</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2001-06-29</date><risdate>2001</risdate><volume>276</volume><issue>26</issue><spage>23785</spage><epage>23789</epage><pages>23785-23789</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A single nucleotide exchange in a promoter region located immediately upstream of the CAAT box of the spinach photosynthesis gene AtpC (gene product is subunit γ of the chloroplast ATP synthase) prevents the formation of a secondary structure and causes an unregulated, constitutive high level of expression (Kusnetsov, V., Landsberger, M., Oelmüller, R. (1999)J. Biol. Chem. 274, 36009–36014). We have isolated cDNAs for ATPC-2, a new polypeptide with homologies to pro- and eukaryotic helicases, which specifically binds to this promoter region. Binding of ATPC-2 competes strongly with that of a CAAT box binding factor (CBF), consistent with the idea that both complexes cannot be formed simultaneously because of sterical reasons. In gel mobility shift assays, high binding activities of ATPC-2 and low binding activities of CBF were observed with nuclear extracts from tissue with low AtpC expression levels, and the opposite was observed with extracts from tissues with high AtpCexpression levels. Binding of ATPC-2 to the mutant sequence, which directs a constitutively high level expression in vivo and prevents the formation of a secondary structure in vitro,is significantly weaker than binding to the wild-type sequence. Again, the opposite results were obtained for the CBF. Thus, we conclude that the assembly of the CBF·DNA complex stimulates transcription of AtpC and that CBF binding is prevented if ATPC-2 is bound to the promoter region. The novel mechanism of gene regulation and the role of the helicase-like protein ATPC-2 as a potential transcriptional repressor is discussed in relation to its modular structure.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11274172</pmid><doi>10.1074/jbc.M010945200</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Arabidopsis - genetics ATPC-2 protein CCAAT-Binding Factor - metabolism Cloning, Molecular DNA Helicases - genetics DNA Helicases - physiology DNA-Binding Proteins - genetics DNA-Binding Proteins - physiology Eukaryotic Cells - metabolism Gene Expression Regulation, Plant Macromolecular Substances Molecular Sequence Data Photosynthesis Plant Proteins - genetics Plant Proteins - physiology Prokaryotic Cells - metabolism Promoter Regions, Genetic Proton-Translocating ATPases - genetics Repressor Proteins - genetics Repressor Proteins - physiology Response Elements Sequence Homology, Amino Acid Spinacia oleracea |
title | A Repressor with Similarities to Prokaryotic and Eukaryotic DNA Helicases Controls the Assembly of the CAAT Box Binding Complex at a Photosynthesis Gene Promoter |
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