Structure of the Escherichia coli RNA Polymerase α Subunit Amino- Terminal Domain
The 2.5 angstrom resolution x-ray crystal structure of the Escherichia coli RNA polymerase (RNAP) α subunit amino-terminal domain (αNTD), which is necessary and sufficient to dimerize and assemble the other RNAP subunits into a transcriptionally active enzyme and contains all of the sequence element...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1998-07, Vol.281 (5374), p.262-266 |
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| creator | Zhang, Gongyi Darst, Seth A. |
| description | The 2.5 angstrom resolution x-ray crystal structure of the Escherichia coli RNA polymerase (RNAP) α subunit amino-terminal domain (αNTD), which is necessary and sufficient to dimerize and assemble the other RNAP subunits into a transcriptionally active enzyme and contains all of the sequence elements conserved among eukaryotic α homologs, has been determined. The αNTD monomer comprises two distinct, flexibly linked domains, only one of which participates in the dimer interface. In the αNTD dimer, a pair of helices from one monomer interact with the cognate helices of the other to form an extensive hydrophobic core. All of the determinants for interactions with the other RNAP subunits lie on one face of the αNTD dimer. Sequence alignments, combined with secondary-structure predictions, support proposals that a heterodimer of the eukaryotic RNAP subunits related to Saccharomyces cerevisiae Rpb3 and Rpb11 plays the role of the αNTD dimer in prokaryotic RNAP. |
| doi_str_mv | 10.1126/science.281.5374.262 |
| format | Article |
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The αNTD monomer comprises two distinct, flexibly linked domains, only one of which participates in the dimer interface. In the αNTD dimer, a pair of helices from one monomer interact with the cognate helices of the other to form an extensive hydrophobic core. All of the determinants for interactions with the other RNAP subunits lie on one face of the αNTD dimer. Sequence alignments, combined with secondary-structure predictions, support proposals that a heterodimer of the eukaryotic RNAP subunits related to Saccharomyces cerevisiae Rpb3 and Rpb11 plays the role of the αNTD dimer in prokaryotic RNAP.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.281.5374.262</identifier><identifier>PMID: 9657722</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Chloroplasts ; Crystallography, X-Ray ; Crystals ; Dimerization ; Dimers ; DNA-Directed RNA Polymerases - chemistry ; Enzymes and enzyme inhibitors ; Escherichia coli ; Escherichia coli - enzymology ; Fundamental and applied biological sciences. Psychology ; Models, Molecular ; Molecular Sequence Data ; Molecules ; Monomers ; Physiological aspects ; Promoter regions ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; RNA ; RNA Polymerase II - chemistry ; RNA polymerases ; Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Transferases</subject><ispartof>Science (American Association for the Advancement of Science), 1998-07, Vol.281 (5374), p.262-266</ispartof><rights>Copyright 1998 American Association for the Advancement of Science</rights><rights>1998 INIST-CNRS</rights><rights>COPYRIGHT 1998 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1998 American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c627t-4e2ee6500eed4be2e4645b2407627102b2e764de18926e58febaae606f55a8623</citedby><cites>FETCH-LOGICAL-c627t-4e2ee6500eed4be2e4645b2407627102b2e764de18926e58febaae606f55a8623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2896023$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2896023$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2334807$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9657722$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Gongyi</creatorcontrib><creatorcontrib>Darst, Seth A.</creatorcontrib><title>Structure of the Escherichia coli RNA Polymerase α Subunit Amino- Terminal Domain</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The 2.5 angstrom resolution x-ray crystal structure of the Escherichia coli RNA polymerase (RNAP) α subunit amino-terminal domain (αNTD), which is necessary and sufficient to dimerize and assemble the other RNAP subunits into a transcriptionally active enzyme and contains all of the sequence elements conserved among eukaryotic α homologs, has been determined. The αNTD monomer comprises two distinct, flexibly linked domains, only one of which participates in the dimer interface. In the αNTD dimer, a pair of helices from one monomer interact with the cognate helices of the other to form an extensive hydrophobic core. All of the determinants for interactions with the other RNAP subunits lie on one face of the αNTD dimer. Sequence alignments, combined with secondary-structure predictions, support proposals that a heterodimer of the eukaryotic RNAP subunits related to Saccharomyces cerevisiae Rpb3 and Rpb11 plays the role of the αNTD dimer in prokaryotic RNAP.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chloroplasts</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Dimerization</subject><subject>Dimers</subject><subject>DNA-Directed RNA Polymerases - chemistry</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>Monomers</subject><subject>Physiological aspects</subject><subject>Promoter regions</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>RNA</subject><subject>RNA Polymerase II - chemistry</subject><subject>RNA polymerases</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Sequence Alignment</subject><subject>Transferases</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0t1q2zAYBmAxVrqs2x10oIMxdlBnsizJ1mGWdVkhNKPpdipk5XOiYlutZMN6WbuRXdOUxbQEAgs-8M_7yEh8L0LnKRmnKRWfgrHQGhjTIh3zLGdjKugLNEqJ5ImkJHuJRoRkIilIzl-h1yHcERIzmZ2iUyl4nlM6QjfLzvem6z1gV-FuA_gymA14azZWY-Nqi2-uJ_i7qx8b8DoA_vMbL_uyb22HJ41tXYJvwccHXeMvrtG2fYNOKl0HeDvcz9CPr5e302_JfDG7mk7miRE07xIGFEBwQgBWrIwvTDBeUkbyGKeElhRywVaQFpIK4EUFpdYgiKg414Wg2Rn6sPvvvXcPPYRONTYYqGvdguuDyqWUrGDyvzAVLOOcZBFe7OBa16BsW7nOa7OGNp68di1UNn6eUCJzTth2A8kBHq8VNNYc8h_3fCQd_OrWug9BXS2vj6aLn0fTz7NjaTGb79GLQzQWooY1qDjI6WKPsx033oXgoVL33jbaP6qUqG1b1dBWFduqtm1V9N8I3w2T6csGVk-LhnrG_P2Q62B0XXndGhueGM0yFtsd2fmO3YXO-ee4kIJE8xcp-_fi</recordid><startdate>19980710</startdate><enddate>19980710</enddate><creator>Zhang, Gongyi</creator><creator>Darst, Seth A.</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>7QL</scope><scope>7TM</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19980710</creationdate><title>Structure of the Escherichia coli RNA Polymerase α Subunit Amino- Terminal Domain</title><author>Zhang, Gongyi ; Darst, Seth A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c627t-4e2ee6500eed4be2e4645b2407627102b2e764de18926e58febaae606f55a8623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chloroplasts</topic><topic>Crystallography, X-Ray</topic><topic>Crystals</topic><topic>Dimerization</topic><topic>Dimers</topic><topic>DNA-Directed RNA Polymerases - chemistry</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Molecules</topic><topic>Monomers</topic><topic>Physiological aspects</topic><topic>Promoter regions</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>RNA</topic><topic>RNA Polymerase II - chemistry</topic><topic>RNA polymerases</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Sequence Alignment</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Gongyi</creatorcontrib><creatorcontrib>Darst, Seth A.</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>Gale In Context: High School</collection><collection>Gale In Context: Biography</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Canada</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Gongyi</au><au>Darst, Seth A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of the Escherichia coli RNA Polymerase α Subunit Amino- Terminal Domain</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1998-07-10</date><risdate>1998</risdate><volume>281</volume><issue>5374</issue><spage>262</spage><epage>266</epage><pages>262-266</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The 2.5 angstrom resolution x-ray crystal structure of the Escherichia coli RNA polymerase (RNAP) α subunit amino-terminal domain (αNTD), which is necessary and sufficient to dimerize and assemble the other RNAP subunits into a transcriptionally active enzyme and contains all of the sequence elements conserved among eukaryotic α homologs, has been determined. The αNTD monomer comprises two distinct, flexibly linked domains, only one of which participates in the dimer interface. In the αNTD dimer, a pair of helices from one monomer interact with the cognate helices of the other to form an extensive hydrophobic core. All of the determinants for interactions with the other RNAP subunits lie on one face of the αNTD dimer. Sequence alignments, combined with secondary-structure predictions, support proposals that a heterodimer of the eukaryotic RNAP subunits related to Saccharomyces cerevisiae Rpb3 and Rpb11 plays the role of the αNTD dimer in prokaryotic RNAP.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>9657722</pmid><doi>10.1126/science.281.5374.262</doi><tpages>5</tpages></addata></record> |
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| ispartof | Science (American Association for the Advancement of Science), 1998-07, Vol.281 (5374), p.262-266 |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Amino Acid Sequence Amino acids Analytical, structural and metabolic biochemistry Biological and medical sciences Chloroplasts Crystallography, X-Ray Crystals Dimerization Dimers DNA-Directed RNA Polymerases - chemistry Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Models, Molecular Molecular Sequence Data Molecules Monomers Physiological aspects Promoter regions Protein Conformation Protein Folding Protein Structure, Secondary RNA RNA Polymerase II - chemistry RNA polymerases Saccharomyces cerevisiae Proteins Sequence Alignment Transferases |
| title | Structure of the Escherichia coli RNA Polymerase α Subunit Amino- Terminal Domain |
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