How Proteins Recognize the TATA Box
The crystal structure of a complex of human TATA-binding protein with TATA-sequence DNA has been solved, complementing earlier TBP/DNA analyses from Saccharomyces cerevisiaeand Arabidopsis thaliana. Special insight into TATA box specificity is provided by considering the TBP/DNA complex, not as a pr...
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| Veröffentlicht in: | Journal of molecular biology 1996-08, Vol.261 (2), p.239-254 |
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| container_end_page | 254 |
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| container_issue | 2 |
| container_start_page | 239 |
| container_title | Journal of molecular biology |
| container_volume | 261 |
| creator | Juo, Zong Sean Chiu, Thang Kien Leiberman, Paul M. Baikalov, Igor Berk, Arnold J. Dickerson, Richard E. |
| description | The crystal structure of a complex of human TATA-binding protein with TATA-sequence DNA has been solved, complementing earlier TBP/DNA analyses from
Saccharomyces cerevisiaeand
Arabidopsis thaliana. Special insight into TATA box specificity is provided by considering the TBP/DNA complex, not as a protein molecule with bound DNA, but as a DNA duplex with a particularly large minor groove ligand. This point of view provides explanations for: (1) why T·A base-pairs are required rather than C·G; (2) why an alternation of T and A bases is needed; (3) how TBP recognizes the upstream and downstream ends of the TATA box in order to bind properly; and (4) why the second half of the TATA box can be more variable than the first. |
| doi_str_mv | 10.1006/jmbi.1996.0456 |
| format | Article |
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Saccharomyces cerevisiaeand
Arabidopsis thaliana. Special insight into TATA box specificity is provided by considering the TBP/DNA complex, not as a protein molecule with bound DNA, but as a DNA duplex with a particularly large minor groove ligand. This point of view provides explanations for: (1) why T·A base-pairs are required rather than C·G; (2) why an alternation of T and A bases is needed; (3) how TBP recognizes the upstream and downstream ends of the TATA box in order to bind properly; and (4) why the second half of the TATA box can be more variable than the first.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1006/jmbi.1996.0456</identifier><identifier>PMID: 8757291</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>A-tract bending ; Amino Acid Sequence ; amino acid sequences ; Arabidopsis ; Arabidopsis thaliana ; Base Sequence ; binding ; binding sites ; crystal structure ; Crystallography, X-Ray ; DNA ; DNA - chemistry ; DNA - metabolism ; DNA bending ; DNA sequence recognition ; DNA-binding proteins ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Humans ; Models, Molecular ; molecular conformation ; Molecular Sequence Data ; Nucleic Acid Conformation ; nucleotide sequences ; Protein Binding ; Protein Conformation ; Saccharomyces ; Saccharomyces cerevisiae ; TATA Box ; TATA-binding proteins ; TATA-Box Binding Protein ; Transcription Factors - chemistry ; Transcription Factors - metabolism ; X-ray diffraction</subject><ispartof>Journal of molecular biology, 1996-08, Vol.261 (2), p.239-254</ispartof><rights>1996 Academic Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-3ae7f0b5ff05226c3413947b780429038de2d4fc8443febfa230e69cc73fbcd03</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/jmbi.1996.0456$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8757291$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Juo, Zong Sean</creatorcontrib><creatorcontrib>Chiu, Thang Kien</creatorcontrib><creatorcontrib>Leiberman, Paul M.</creatorcontrib><creatorcontrib>Baikalov, Igor</creatorcontrib><creatorcontrib>Berk, Arnold J.</creatorcontrib><creatorcontrib>Dickerson, Richard E.</creatorcontrib><title>How Proteins Recognize the TATA Box</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The crystal structure of a complex of human TATA-binding protein with TATA-sequence DNA has been solved, complementing earlier TBP/DNA analyses from
Saccharomyces cerevisiaeand
Arabidopsis thaliana. Special insight into TATA box specificity is provided by considering the TBP/DNA complex, not as a protein molecule with bound DNA, but as a DNA duplex with a particularly large minor groove ligand. This point of view provides explanations for: (1) why T·A base-pairs are required rather than C·G; (2) why an alternation of T and A bases is needed; (3) how TBP recognizes the upstream and downstream ends of the TATA box in order to bind properly; and (4) why the second half of the TATA box can be more variable than the first.</description><subject>A-tract bending</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Arabidopsis</subject><subject>Arabidopsis thaliana</subject><subject>Base Sequence</subject><subject>binding</subject><subject>binding sites</subject><subject>crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>DNA bending</subject><subject>DNA sequence recognition</subject><subject>DNA-binding proteins</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>molecular conformation</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>nucleotide sequences</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Saccharomyces</subject><subject>Saccharomyces cerevisiae</subject><subject>TATA Box</subject><subject>TATA-binding proteins</subject><subject>TATA-Box Binding Protein</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><subject>X-ray diffraction</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMotVav3sQFwdvWycdukmMtfoGgaHsOu9mJRtpGk61fv94uLd7E0xzeZ95hHkIOKQwpQHn2Mq_9kGpdDkEU5RbpU1A6VyVX26QPwFjOFC93yV5KLwBQcKF6pKdkIZmmfXJyHT6y-xha9IuUPaANTwv_jVn7jNlkNBll5-Fzn-y4apbwYDMHZHp5MRlf57d3Vzfj0W1uBRdtziuUDurCOSgYKy0XlGsha6lAMA1cNcga4awSgjusXcU4YKmtldzVtgE-IKfr3tcY3paYWjP3yeJsVi0wLJORigmqmf4XpEUpgcoOHK5BG0NKEZ15jX5exS9DwXT6TKfPdPpMp2-1cLRpXtZzbH7xja9VfrzOXRVM9RR9MtNHBpQDLRjtPh4QtSZwZerdYzTJelxYbHxE25om-L-O_wDhvYUY</recordid><startdate>19960816</startdate><enddate>19960816</enddate><creator>Juo, Zong Sean</creator><creator>Chiu, Thang Kien</creator><creator>Leiberman, Paul M.</creator><creator>Baikalov, Igor</creator><creator>Berk, Arnold J.</creator><creator>Dickerson, Richard E.</creator><general>Elsevier Ltd</general><scope>FBQ</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>19960816</creationdate><title>How Proteins Recognize the TATA Box</title><author>Juo, Zong Sean ; 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Saccharomyces cerevisiaeand
Arabidopsis thaliana. Special insight into TATA box specificity is provided by considering the TBP/DNA complex, not as a protein molecule with bound DNA, but as a DNA duplex with a particularly large minor groove ligand. This point of view provides explanations for: (1) why T·A base-pairs are required rather than C·G; (2) why an alternation of T and A bases is needed; (3) how TBP recognizes the upstream and downstream ends of the TATA box in order to bind properly; and (4) why the second half of the TATA box can be more variable than the first.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>8757291</pmid><doi>10.1006/jmbi.1996.0456</doi><tpages>16</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 1996-08, Vol.261 (2), p.239-254 |
| issn | 0022-2836 1089-8638 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78241929 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | A-tract bending Amino Acid Sequence amino acid sequences Arabidopsis Arabidopsis thaliana Base Sequence binding binding sites crystal structure Crystallography, X-Ray DNA DNA - chemistry DNA - metabolism DNA bending DNA sequence recognition DNA-binding proteins DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Humans Models, Molecular molecular conformation Molecular Sequence Data Nucleic Acid Conformation nucleotide sequences Protein Binding Protein Conformation Saccharomyces Saccharomyces cerevisiae TATA Box TATA-binding proteins TATA-Box Binding Protein Transcription Factors - chemistry Transcription Factors - metabolism X-ray diffraction |
| title | How Proteins Recognize the TATA Box |
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