Secondary Structure of the ETS Domain Places Murine Ets-1 in the Superfamily of Winged Helix-Turn-Helix DNA-Binding Proteins
The members of the ets gene family of transcription factors are characterized by a conserved 85-residue DNA-binding region, termed the ETS domain, that lacks sequence homology to structurally characterized DNA-binding motifs. The secondary structure of the ETS domain of murine Ets-1 was determined o...
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| Veröffentlicht in: | Biochemistry (Easton) 1994-11, Vol.33 (46), p.13509-13516 |
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| container_title | Biochemistry (Easton) |
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| creator | Donaldson, Logan W Petersen, Jeannine M Graves, Barbara J McIntosh, Lawrence P |
| description | The members of the ets gene family of transcription factors are characterized by a conserved 85-residue DNA-binding region, termed the ETS domain, that lacks sequence homology to structurally characterized DNA-binding motifs. The secondary structure of the ETS domain of murine Ets-1 was determined on the basis of NMR chemical shifts, NOE and J-coupling constraints, amide hydrogen exchange, circular dichroism, and FT-IR spectroscopy. The ETS domain is composed of three alpha-helices (H) and four beta-strands (S) arranged in the order H1-S1-S2-H2-H3-S3-S4. The four-stranded antiparallel beta-sheet is the scaffold for a putative helix-turn-helix DNA recognition motif formed by helices 2 and 3. The 25 residues extending beyond the ETS domain to the native C-terminus of the truncated Ets-1 also contain a helical segment. On the basis of the similarity of this topology with that of catabolite activator protein (CAP), heat shock factor (HSF), and hepatocyte nuclear factor (HNF-3 gamma), we propose that ets proteins are members of the superfamily of winged helix-turn-helix DNA-binding proteins. |
| doi_str_mv | 10.1021/bi00250a001 |
| format | Article |
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The secondary structure of the ETS domain of murine Ets-1 was determined on the basis of NMR chemical shifts, NOE and J-coupling constraints, amide hydrogen exchange, circular dichroism, and FT-IR spectroscopy. The ETS domain is composed of three alpha-helices (H) and four beta-strands (S) arranged in the order H1-S1-S2-H2-H3-S3-S4. The four-stranded antiparallel beta-sheet is the scaffold for a putative helix-turn-helix DNA recognition motif formed by helices 2 and 3. The 25 residues extending beyond the ETS domain to the native C-terminus of the truncated Ets-1 also contain a helical segment. On the basis of the similarity of this topology with that of catabolite activator protein (CAP), heat shock factor (HSF), and hepatocyte nuclear factor (HNF-3 gamma), we propose that ets proteins are members of the superfamily of winged helix-turn-helix DNA-binding proteins.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00250a001</identifier><identifier>PMID: 7947760</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Sequence ; Animals ; Circular Dichroism ; Cloning, Molecular ; DNA-Binding Proteins - chemistry ; Escherichia coli ; Helix-Loop-Helix Motifs ; Hydrogen - chemistry ; Magnetic Resonance Spectroscopy ; Mice ; Molecular Sequence Data ; Protein Structure, Secondary ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins - chemistry ; Proto-Oncogene Proteins - genetics ; Proto-Oncogene Proteins c-ets ; Recombinant Proteins ; Sequence Homology, Amino Acid ; Transcription Factors</subject><ispartof>Biochemistry (Easton), 1994-11, Vol.33 (46), p.13509-13516</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a480t-2da48f2da8d0893a75aa5c43cd054ed69e44774b95ee8f1d60916691ae9efd883</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00250a001$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00250a001$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2763,27074,27922,27923,56736,56786</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7947760$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Donaldson, Logan W</creatorcontrib><creatorcontrib>Petersen, Jeannine M</creatorcontrib><creatorcontrib>Graves, Barbara J</creatorcontrib><creatorcontrib>McIntosh, Lawrence P</creatorcontrib><title>Secondary Structure of the ETS Domain Places Murine Ets-1 in the Superfamily of Winged Helix-Turn-Helix DNA-Binding Proteins</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The members of the ets gene family of transcription factors are characterized by a conserved 85-residue DNA-binding region, termed the ETS domain, that lacks sequence homology to structurally characterized DNA-binding motifs. The secondary structure of the ETS domain of murine Ets-1 was determined on the basis of NMR chemical shifts, NOE and J-coupling constraints, amide hydrogen exchange, circular dichroism, and FT-IR spectroscopy. The ETS domain is composed of three alpha-helices (H) and four beta-strands (S) arranged in the order H1-S1-S2-H2-H3-S3-S4. The four-stranded antiparallel beta-sheet is the scaffold for a putative helix-turn-helix DNA recognition motif formed by helices 2 and 3. The 25 residues extending beyond the ETS domain to the native C-terminus of the truncated Ets-1 also contain a helical segment. On the basis of the similarity of this topology with that of catabolite activator protein (CAP), heat shock factor (HSF), and hepatocyte nuclear factor (HNF-3 gamma), we propose that ets proteins are members of the superfamily of winged helix-turn-helix DNA-binding proteins.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Circular Dichroism</subject><subject>Cloning, Molecular</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>Escherichia coli</subject><subject>Helix-Loop-Helix Motifs</subject><subject>Hydrogen - chemistry</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Protein Structure, Secondary</subject><subject>Proto-Oncogene Protein c-ets-1</subject><subject>Proto-Oncogene Proteins - chemistry</subject><subject>Proto-Oncogene Proteins - genetics</subject><subject>Proto-Oncogene Proteins c-ets</subject><subject>Recombinant Proteins</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transcription Factors</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhS0EKkNhxRrJK1ggw3XiR7zsCwoUmCqDkNhYnvgG3OYx2InUSvx4PMyoYoHExtf2-e6xfC4hTzm84lDw1-sAUEhwAPweWXBZABPGyPtkAQCKFUbBQ_Iopat8FKDFATnQRmitYEF-1diMg3fxltZTnJtpjkjHlk4_kJ6tano69i4MdNm5BhP9OMcwZGFKjNN8vaXqeYOxdX3obreNX8PwHT09xy7csNUcB_ZnS08_HbHjMPgs02UcJwxDekwetK5L-GRfD8mXN2erk3N28fntu5OjC-ZEBRMrfK5tXisPlSmdls7JRpSNBynQK4Mi_0asjUSsWu4VGK6U4Q4Ntr6qykPyfOe7iePPGdNk-5Aa7Do34Dgnq5U2Wkv5XzDbal2WPIMvd2ATx5QitnYTQ59TtBzsdij2r6Fk-tnedl736O_Y_RSyznZ6SBPe3MkuXlulSy3talnb8tvl-_LD8aXd-r3Y8a5J9mrMIef0_vnyb-4TofY</recordid><startdate>19941101</startdate><enddate>19941101</enddate><creator>Donaldson, Logan W</creator><creator>Petersen, Jeannine M</creator><creator>Graves, Barbara J</creator><creator>McIntosh, Lawrence P</creator><general>American Chemical Society</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>7TM</scope><scope>7TO</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19941101</creationdate><title>Secondary Structure of the ETS Domain Places Murine Ets-1 in the Superfamily of Winged Helix-Turn-Helix DNA-Binding Proteins</title><author>Donaldson, Logan W ; Petersen, Jeannine M ; Graves, Barbara J ; McIntosh, Lawrence P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a480t-2da48f2da8d0893a75aa5c43cd054ed69e44774b95ee8f1d60916691ae9efd883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Circular Dichroism</topic><topic>Cloning, Molecular</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>Escherichia coli</topic><topic>Helix-Loop-Helix Motifs</topic><topic>Hydrogen - chemistry</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Protein Structure, Secondary</topic><topic>Proto-Oncogene Protein c-ets-1</topic><topic>Proto-Oncogene Proteins - chemistry</topic><topic>Proto-Oncogene Proteins - genetics</topic><topic>Proto-Oncogene Proteins c-ets</topic><topic>Recombinant Proteins</topic><topic>Sequence Homology, Amino Acid</topic><topic>Transcription Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Donaldson, Logan W</creatorcontrib><creatorcontrib>Petersen, Jeannine M</creatorcontrib><creatorcontrib>Graves, Barbara J</creatorcontrib><creatorcontrib>McIntosh, Lawrence P</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>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Donaldson, Logan W</au><au>Petersen, Jeannine M</au><au>Graves, Barbara J</au><au>McIntosh, Lawrence P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Secondary Structure of the ETS Domain Places Murine Ets-1 in the Superfamily of Winged Helix-Turn-Helix DNA-Binding Proteins</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1994-11-01</date><risdate>1994</risdate><volume>33</volume><issue>46</issue><spage>13509</spage><epage>13516</epage><pages>13509-13516</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The members of the ets gene family of transcription factors are characterized by a conserved 85-residue DNA-binding region, termed the ETS domain, that lacks sequence homology to structurally characterized DNA-binding motifs. The secondary structure of the ETS domain of murine Ets-1 was determined on the basis of NMR chemical shifts, NOE and J-coupling constraints, amide hydrogen exchange, circular dichroism, and FT-IR spectroscopy. The ETS domain is composed of three alpha-helices (H) and four beta-strands (S) arranged in the order H1-S1-S2-H2-H3-S3-S4. The four-stranded antiparallel beta-sheet is the scaffold for a putative helix-turn-helix DNA recognition motif formed by helices 2 and 3. The 25 residues extending beyond the ETS domain to the native C-terminus of the truncated Ets-1 also contain a helical segment. On the basis of the similarity of this topology with that of catabolite activator protein (CAP), heat shock factor (HSF), and hepatocyte nuclear factor (HNF-3 gamma), we propose that ets proteins are members of the superfamily of winged helix-turn-helix DNA-binding proteins.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>7947760</pmid><doi>10.1021/bi00250a001</doi><tpages>8</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Circular Dichroism Cloning, Molecular DNA-Binding Proteins - chemistry Escherichia coli Helix-Loop-Helix Motifs Hydrogen - chemistry Magnetic Resonance Spectroscopy Mice Molecular Sequence Data Protein Structure, Secondary Proto-Oncogene Protein c-ets-1 Proto-Oncogene Proteins - chemistry Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins c-ets Recombinant Proteins Sequence Homology, Amino Acid Transcription Factors |
| title | Secondary Structure of the ETS Domain Places Murine Ets-1 in the Superfamily of Winged Helix-Turn-Helix DNA-Binding Proteins |
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