A new family of plant transcription factors displays a novel ssDNA-binding surface
The crystal structure of p24, the single-stranded DNA (ssDNA) binding subunit of the plant defense transcription factor PBF-2, has been determined to 2.3 Å resolution. p24 is representative of a novel family of ubiquitous plant-specific proteins that we refer to as the Whirly family because of their...
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| Veröffentlicht in: | Nature Structural Biology 2002-07, Vol.9 (7), p.512-517 |
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| creator | Brisson, Normand Sygusch, Jurgen Desveaux, Darrell Allard, Julie |
| description | The crystal structure of p24, the single-stranded DNA (ssDNA) binding subunit of the plant defense transcription factor PBF-2, has been determined to 2.3 Å resolution. p24 is representative of a novel family of ubiquitous plant-specific proteins that we refer to as the Whirly family because of their quaternary structure. PBF-2 is composed of four p24 molecules that interact through a helix-loop-helix motif. This interaction produces a central pore, with β-strands radiating outwards, resulting in a whirligig appearance to the quaternary structure. The noncrystallographic C4 symmetry arrangement of p24 subunits is novel for ssDNA binding proteins and may explain the binding specificity of PBF-2. This structural arrangement also supports the role of PBF-2 in binding melted promoter regions to modulate gene expression. |
| doi_str_mv | 10.1038/nsb814 |
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PBF-2 is composed of four p24 molecules that interact through a helix-loop-helix motif. This interaction produces a central pore, with β-strands radiating outwards, resulting in a whirligig appearance to the quaternary structure. The noncrystallographic C4 symmetry arrangement of p24 subunits is novel for ssDNA binding proteins and may explain the binding specificity of PBF-2. This structural arrangement also supports the role of PBF-2 in binding melted promoter regions to modulate gene expression.</description><identifier>ISSN: 1072-8368</identifier><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 2331-365X</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsb814</identifier><identifier>PMID: 12080340</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Amino Acid Sequence ; Binding Sites ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Blotting, Western ; Chromatography, Gel ; Conserved Sequence ; Crystallography, X-Ray ; DNA ; DNA, Single-Stranded - chemistry ; DNA, Single-Stranded - genetics ; DNA, Single-Stranded - metabolism ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Electrophoretic Mobility Shift Assay ; Gene Expression Regulation, Plant ; Helix-Loop-Helix Motifs ; letter ; Life Sciences ; Membrane Biology ; Models, Molecular ; Molecular Sequence Data ; NATIONAL SYNCHROTRON LIGHT SOURCE ; NSLS ; Nuclear Proteins - chemistry ; Nuclear Proteins - metabolism ; PARTICLE ACCELERATORS ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Plants - chemistry ; Protein Structure ; Protein Structure, Quaternary ; Protein Structure, Secondary ; TRANSCRIPTION FACTORS ; Transcription Factors - chemistry ; Transcription Factors - metabolism</subject><ispartof>Nature Structural Biology, 2002-07, Vol.9 (7), p.512-517</ispartof><rights>Springer Nature America, Inc. 2002</rights><rights>Copyright Nature Publishing Group Jul 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c414t-b4138fc74a918fa6d898e12cd9f933a159ec503d0995e6442fcdfea14a27fb793</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,885,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12080340$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/15008874$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Brisson, Normand</creatorcontrib><creatorcontrib>Sygusch, Jurgen</creatorcontrib><creatorcontrib>Desveaux, Darrell</creatorcontrib><creatorcontrib>Allard, Julie</creatorcontrib><creatorcontrib>Brookhaven National Laboratory, National Synchrotron Light Source (US)</creatorcontrib><title>A new family of plant transcription factors displays a novel ssDNA-binding surface</title><title>Nature Structural Biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Biol</addtitle><description>The crystal structure of p24, the single-stranded DNA (ssDNA) binding subunit of the plant defense transcription factor PBF-2, has been determined to 2.3 Å resolution. p24 is representative of a novel family of ubiquitous plant-specific proteins that we refer to as the Whirly family because of their quaternary structure. PBF-2 is composed of four p24 molecules that interact through a helix-loop-helix motif. This interaction produces a central pore, with β-strands radiating outwards, resulting in a whirligig appearance to the quaternary structure. The noncrystallographic C4 symmetry arrangement of p24 subunits is novel for ssDNA binding proteins and may explain the binding specificity of PBF-2. This structural arrangement also supports the role of PBF-2 in binding melted promoter regions to modulate gene expression.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Blotting, Western</subject><subject>Chromatography, Gel</subject><subject>Conserved Sequence</subject><subject>Crystallography, X-Ray</subject><subject>DNA</subject><subject>DNA, Single-Stranded - chemistry</subject><subject>DNA, Single-Stranded - genetics</subject><subject>DNA, Single-Stranded - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Electrophoretic Mobility Shift Assay</subject><subject>Gene Expression Regulation, Plant</subject><subject>Helix-Loop-Helix Motifs</subject><subject>letter</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>NATIONAL SYNCHROTRON LIGHT SOURCE</subject><subject>NSLS</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - metabolism</subject><subject>PARTICLE ACCELERATORS</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - metabolism</subject><subject>Plants - chemistry</subject><subject>Protein Structure</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Secondary</subject><subject>TRANSCRIPTION FACTORS</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><issn>1072-8368</issn><issn>1545-9993</issn><issn>2331-365X</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0U9LHDEYBvBQLHW19ROIBAv1NG3-zU5yXKzVglgoLfQWMpnERmaTNW_Gst_elFkU7KGnHJ4fT3h5EDqi5CMlXH6K0EsqXqEF45w2fNn-2kMLSjrWSL6U--gA4I4QKgRRb9A-ZUQSLsgCfV_h6P5gb9Zh3OLk8WY0seCSTQSbw6aEFGtqS8qAhwA13gI2OKYHN2KAzzerpg9xCPEWw5SrdG_Ra29GcO927yH6-eXix_lVc_3t8uv56rqxgorS9IJy6W0njKLSm-UglXSU2UF5xbmhrXK2JXwgSrVuKQTzdvDOUGFY5_tO8UP0fu5NUIIGG4qzv22K0dmiaUuIlJ2o6sOsNjndTw6KXgewbqxnujSB7qhsBWH0v7A6TlrOKzx9Ae_SlGM9VTMmOVe8yqc2mxNAdl5vclibvNWU6L-L6XmxCk92bVO_dsMz201UwdkMoEbx1uXn7_6pOp5lNGXK7qlqFz8CSVamrg</recordid><startdate>20020701</startdate><enddate>20020701</enddate><creator>Brisson, Normand</creator><creator>Sygusch, Jurgen</creator><creator>Desveaux, Darrell</creator><creator>Allard, Julie</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</general><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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20020701</creationdate><title>A new family of plant transcription factors displays a novel ssDNA-binding surface</title><author>Brisson, Normand ; Sygusch, Jurgen ; Desveaux, Darrell ; Allard, Julie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c414t-b4138fc74a918fa6d898e12cd9f933a159ec503d0995e6442fcdfea14a27fb793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>Blotting, Western</topic><topic>Chromatography, Gel</topic><topic>Conserved Sequence</topic><topic>Crystallography, X-Ray</topic><topic>DNA</topic><topic>DNA, Single-Stranded - 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Academic</collection><collection>OSTI.GOV</collection><jtitle>Nature Structural Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brisson, Normand</au><au>Sygusch, Jurgen</au><au>Desveaux, Darrell</au><au>Allard, Julie</au><aucorp>Brookhaven National Laboratory, National Synchrotron Light Source (US)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A new family of plant transcription factors displays a novel ssDNA-binding surface</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>2002-07-01</date><risdate>2002</risdate><volume>9</volume><issue>7</issue><spage>512</spage><epage>517</epage><pages>512-517</pages><issn>1072-8368</issn><issn>1545-9993</issn><eissn>2331-365X</eissn><eissn>1545-9985</eissn><abstract>The crystal structure of p24, the single-stranded DNA (ssDNA) binding subunit of the plant defense transcription factor PBF-2, has been determined to 2.3 Å resolution. p24 is representative of a novel family of ubiquitous plant-specific proteins that we refer to as the Whirly family because of their quaternary structure. PBF-2 is composed of four p24 molecules that interact through a helix-loop-helix motif. This interaction produces a central pore, with β-strands radiating outwards, resulting in a whirligig appearance to the quaternary structure. The noncrystallographic C4 symmetry arrangement of p24 subunits is novel for ssDNA binding proteins and may explain the binding specificity of PBF-2. This structural arrangement also supports the role of PBF-2 in binding melted promoter regions to modulate gene expression.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>12080340</pmid><doi>10.1038/nsb814</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino Acid Sequence Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences Blotting, Western Chromatography, Gel Conserved Sequence Crystallography, X-Ray DNA DNA, Single-Stranded - chemistry DNA, Single-Stranded - genetics DNA, Single-Stranded - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Electrophoretic Mobility Shift Assay Gene Expression Regulation, Plant Helix-Loop-Helix Motifs letter Life Sciences Membrane Biology Models, Molecular Molecular Sequence Data NATIONAL SYNCHROTRON LIGHT SOURCE NSLS Nuclear Proteins - chemistry Nuclear Proteins - metabolism PARTICLE ACCELERATORS Plant Proteins - chemistry Plant Proteins - metabolism Plants - chemistry Protein Structure Protein Structure, Quaternary Protein Structure, Secondary TRANSCRIPTION FACTORS Transcription Factors - chemistry Transcription Factors - metabolism |
| title | A new family of plant transcription factors displays a novel ssDNA-binding surface |
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