Structural Biology of RNA Polymerase III: Subcomplex C17/25 X-Ray Structure and 11 Subunit Enzyme Model
We obtained an 11 subunit model of RNA polymerase (Pol) III by combining a homology model of the nine subunit core enzyme with a new X-ray structure of the subcomplex C17/25. Compared to Pol II, Pol III shows a conserved active center for RNA synthesis but a structurally different upstream face for...
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| Veröffentlicht in: | Molecular cell 2006-07, Vol.23 (1), p.71-81 |
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| creator | Jasiak, Anna J. Armache, Karim-Jean Martens, Birgit Jansen, Ralf-Peter Cramer, Patrick |
| description | We obtained an 11 subunit model of RNA polymerase (Pol) III by combining a homology model of the nine subunit core enzyme with a new X-ray structure of the subcomplex C17/25. Compared to Pol II, Pol III shows a conserved active center for RNA synthesis but a structurally different upstream face for specific initiation complex assembly during promoter selection. The Pol III upstream face includes a HRDC domain in subunit C17 that is translated by 35 Å and rotated by 150° compared to its Pol II counterpart. The HRDC domain is essential in vivo, folds independently in vitro, and, unlike other HRDC domains, shows no indication of nucleic acid binding. Thus, the HRDC domain is a functional module that could account for the role of C17 in Pol III promoter-specific initiation. During elongation, C17/25 may bind Pol III transcripts emerging from the adjacent exit pore, because the subcomplex binds to tRNA in vitro. |
| doi_str_mv | 10.1016/j.molcel.2006.05.013 |
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Compared to Pol II, Pol III shows a conserved active center for RNA synthesis but a structurally different upstream face for specific initiation complex assembly during promoter selection. The Pol III upstream face includes a HRDC domain in subunit C17 that is translated by 35 Å and rotated by 150° compared to its Pol II counterpart. The HRDC domain is essential in vivo, folds independently in vitro, and, unlike other HRDC domains, shows no indication of nucleic acid binding. Thus, the HRDC domain is a functional module that could account for the role of C17 in Pol III promoter-specific initiation. 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Compared to Pol II, Pol III shows a conserved active center for RNA synthesis but a structurally different upstream face for specific initiation complex assembly during promoter selection. The Pol III upstream face includes a HRDC domain in subunit C17 that is translated by 35 Å and rotated by 150° compared to its Pol II counterpart. The HRDC domain is essential in vivo, folds independently in vitro, and, unlike other HRDC domains, shows no indication of nucleic acid binding. Thus, the HRDC domain is a functional module that could account for the role of C17 in Pol III promoter-specific initiation. 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Armache, Karim-Jean ; Martens, Birgit ; Jansen, Ralf-Peter ; Cramer, Patrick</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-a5ed1a1bf2c00fdc621c0e2e85f1ecc80615d5e3c88ff2658b318d1beb74e7d03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Crystallography, X-Ray</topic><topic>DNA</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Binding</topic><topic>Protein Subunits - chemistry</topic><topic>Protein Subunits - genetics</topic><topic>Protein Subunits - physiology</topic><topic>RNA Polymerase II - chemistry</topic><topic>RNA Polymerase II - genetics</topic><topic>RNA Polymerase II - physiology</topic><topic>RNA Polymerase III - chemistry</topic><topic>RNA Polymerase III - genetics</topic><topic>RNA Polymerase III - physiology</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - physiology</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jasiak, Anna J.</creatorcontrib><creatorcontrib>Armache, Karim-Jean</creatorcontrib><creatorcontrib>Martens, Birgit</creatorcontrib><creatorcontrib>Jansen, Ralf-Peter</creatorcontrib><creatorcontrib>Cramer, Patrick</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>MEDLINE - Academic</collection><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jasiak, Anna J.</au><au>Armache, Karim-Jean</au><au>Martens, Birgit</au><au>Jansen, Ralf-Peter</au><au>Cramer, Patrick</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Biology of RNA Polymerase III: Subcomplex C17/25 X-Ray Structure and 11 Subunit Enzyme Model</atitle><jtitle>Molecular cell</jtitle><addtitle>Mol Cell</addtitle><date>2006-07-07</date><risdate>2006</risdate><volume>23</volume><issue>1</issue><spage>71</spage><epage>81</epage><pages>71-81</pages><issn>1097-2765</issn><eissn>1097-4164</eissn><abstract>We obtained an 11 subunit model of RNA polymerase (Pol) III by combining a homology model of the nine subunit core enzyme with a new X-ray structure of the subcomplex C17/25. 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| subjects | Amino Acid Sequence Crystallography, X-Ray DNA Models, Molecular Molecular Sequence Data Protein Binding Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - physiology RNA Polymerase II - chemistry RNA Polymerase II - genetics RNA Polymerase II - physiology RNA Polymerase III - chemistry RNA Polymerase III - genetics RNA Polymerase III - physiology Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - physiology Sequence Alignment |
| title | Structural Biology of RNA Polymerase III: Subcomplex C17/25 X-Ray Structure and 11 Subunit Enzyme Model |
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