Eintrag weiter verarbeiten
Conformational flexibility of RNA polymerase III during transcriptional elongation
Gespeichert in:
| Veröffentlicht in: | The EMBO journal 29(2010), 22, Seite 3762-3772 |
|---|---|
| Personen und Körperschaften: | , |
| Titel: | Conformational flexibility of RNA polymerase III during transcriptional elongation/ Carlos Fernández‐Tornero, Bettina Böttcher, Umar Jan Rashid, Ulrich Steuerwald, Beate Flörchinger, Damien P. Devos, Doris Lindner and Christoph W. Müller |
| Format: | E-Book-Kapitel |
| Sprache: | Englisch |
| veröffentlicht: |
22 October 2010
|
| Gesamtaufnahme: |
European Molecular Biology Organization: The EMBO journal, 29(2010), 22, Seite 3762-3772
, volume:29 |
| Schlagwörter: | |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
| LEADER | 03431caa a2200577 4500 | ||
|---|---|---|---|
| 001 | 0-155867165X | ||
| 003 | DE-627 | ||
| 005 | 20220813173036.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 170516s2010 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1038/emboj.2010.266 |2 doi | |
| 035 | |a (DE-627)155867165X | ||
| 035 | |a (DE-576)488671655 | ||
| 035 | |a (DE-599)BSZ488671655 | ||
| 035 | |a (OCoLC)1340975466 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rda | ||
| 041 | |a eng | ||
| 100 | 1 | |a Fernández‐Tornero, Carlos |e VerfasserIn |0 (DE-588)1132163307 |0 (DE-627)887456839 |0 (DE-576)488671744 |4 aut | |
| 245 | 1 | 0 | |a Conformational flexibility of RNA polymerase III during transcriptional elongation |c Carlos Fernández‐Tornero, Bettina Böttcher, Umar Jan Rashid, Ulrich Steuerwald, Beate Flörchinger, Damien P. Devos, Doris Lindner and Christoph W. Müller |
| 264 | 1 | |c 22 October 2010 | |
| 300 | |a 11 | ||
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Gesehen am 16.05.2017 | ||
| 520 | |a RNA polymerase (Pol) III is responsible for the transcription of genes encoding small RNAs, including tRNA, 5S rRNA and U6 RNA. Here, we report the electron cryomicroscopy structures of yeast Pol III at 9.9 Å resolution and its elongation complex at 16.5 Å resolution. Particle sub‐classification reveals prominent EM densities for the two Pol III‐specific subcomplexes, C31/C82/C34 and C37/C53, that can be interpreted using homology models. While the winged‐helix‐containing C31/C82/C34 subcomplex initiates transcription from one side of the DNA‐binding cleft, the C37/C53 subcomplex accesses the transcription bubble from the opposite side of this cleft. The transcribing Pol III enzyme structure not only shows the complete incoming DNA duplex, but also reveals the exit path of newly synthesized RNA. During transcriptional elongation, the Pol III‐specific subcomplexes tightly enclose the incoming DNA duplex, which likely increases processivity and provides structural insights into the conformational switch between Pol III‐mediated initiation and elongation. | ||
| 650 | 4 | |a electron cryomicroscopy | |
| 650 | 4 | |a elongation complex | |
| 650 | 4 | |a RNA polymerase III | |
| 650 | 4 | |a transcription elongation | |
| 650 | 4 | |a transcription initiation | |
| 700 | 1 | |a Devos, Damien |e VerfasserIn |0 (DE-588)1038353319 |0 (DE-627)766122247 |0 (DE-576)392341069 |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |a European Molecular Biology Organization |t The EMBO journal |d Heidelberg : EMBO Press, 1982 |g 29(2010), 22, Seite 3762-3772 |w (DE-627)266022529 |w (DE-600)1467419-1 |w (DE-576)075961377 |x 1460-2075 |7 nnns |
| 773 | 1 | 8 | |g volume:29 |g year:2010 |g number:22 |g pages:3762-3772 |g extent:11 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1038/emboj.2010.266 |x Verlag |x Resolving-System |z kostenfrei |3 Volltext |
| 856 | 4 | 0 | |u http://emboj.embopress.org/content/29/22/3762 |x Verlag |z kostenfrei |3 Volltext |
| 936 | u | w | |d 29 |j 2010 |e 22 |h 3762-3772 |g 11 |
| 951 | |a AR | ||
| 856 | 4 | 0 | |u http://dx.doi.org/10.1038/emboj.2010.266 |9 LFER |
| 852 | |a LFER |z 2017-06-08T00:00:00Z | ||
| 970 | |c OD | ||
| 971 | |c EBOOK | ||
| 972 | |c EBOOK | ||
| 973 | |c Aufsatz | ||
| 935 | |a lfer | ||
| 900 | |a Devos, Damien P. | ||
| 900 | |a Devos, Damien Paul | ||
| 900 | |a Fernández Tornero, Carlos | ||
| 900 | |a Fernández, Carlos Tornero- | ||
| 951 | |b ZZ | ||
| 980 | |a 155867165X |b 0 |k 155867165X |o 488671655 |c lfer | ||
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Conformational+flexibility+of+RNA+polymerase+III+during+transcriptional+elongation&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rft.creator=Fern%C3%A1ndez%E2%80%90Tornero%2C+Carlos&rft.pub=&rft.format=Journal&rft.language=English&rft.issn=1460-2075 |
|---|
| _version_ | 1757948391498711040 |
|---|---|
| access_facet | Electronic Resources |
| author | Fernández‐Tornero, Carlos, Devos, Damien |
| author_facet | Fernández‐Tornero, Carlos, Devos, Damien |
| author_role | aut, aut |
| author_sort | Fernández‐Tornero, Carlos |
| author_variant | c f cf, d d dd |
| callnumber-sort | |
| collection | lfer |
| container_reference | 29(2010), 22, Seite 3762-3772 |
| container_title | The EMBO journal |
| contents | RNA polymerase (Pol) III is responsible for the transcription of genes encoding small RNAs, including tRNA, 5S rRNA and U6 RNA. Here, we report the electron cryomicroscopy structures of yeast Pol III at 9.9 Å resolution and its elongation complex at 16.5 Å resolution. Particle sub‐classification reveals prominent EM densities for the two Pol III‐specific subcomplexes, C31/C82/C34 and C37/C53, that can be interpreted using homology models. While the winged‐helix‐containing C31/C82/C34 subcomplex initiates transcription from one side of the DNA‐binding cleft, the C37/C53 subcomplex accesses the transcription bubble from the opposite side of this cleft. The transcribing Pol III enzyme structure not only shows the complete incoming DNA duplex, but also reveals the exit path of newly synthesized RNA. During transcriptional elongation, the Pol III‐specific subcomplexes tightly enclose the incoming DNA duplex, which likely increases processivity and provides structural insights into the conformational switch between Pol III‐mediated initiation and elongation. |
| ctrlnum | (DE-627)155867165X, (DE-576)488671655, (DE-599)BSZ488671655, (OCoLC)1340975466 |
| doi_str_mv | 10.1038/emboj.2010.266 |
| facet_avail | Online, Free |
| finc_class_facet | not assigned |
| finc_id_str | 0019050232 |
| footnote | Gesehen am 16.05.2017 |
| format | ElectronicBookComponentPart |
| format_access_txtF_mv | Article, E-Article |
| format_de105 | Ebook |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_del152 | Buch |
| format_detail_txtF_mv | text-online-monograph-child |
| format_dezi4 | e-Book |
| format_finc | Article, E-Article |
| format_legacy | ElectronicBookPart |
| format_strict_txtF_mv | E-Article |
| geogr_code | not assigned |
| geogr_code_person | Other places |
| hierarchy_parent_id | 0-266022529 |
| hierarchy_parent_title | European Molecular Biology Organization: The EMBO journal |
| hierarchy_sequence | 29(2010), 22, Seite 3762-3772 |
| hierarchy_top_id | 0-266022529 |
| hierarchy_top_title | European Molecular Biology Organization: The EMBO journal |
| id | 0-155867165X |
| illustrated | Not Illustrated |
| imprint | 22 October 2010 |
| imprint_str_mv | 22 October 2010 |
| institution | DE-D117, DE-105, LFER, DE-Ch1, DE-15, DE-14, DE-Zwi2 |
| is_hierarchy_id | 0-155867165X |
| is_hierarchy_title | Conformational flexibility of RNA polymerase III during transcriptional elongation |
| isil_str_mv | LFER |
| issn | 1460-2075 |
| kxp_id_str | 155867165X |
| language | English |
| last_indexed | 2023-02-16T01:17:09.765Z |
| local_heading_facet_dezwi2 | electron cryomicroscopy, elongation complex, RNA polymerase III, transcription elongation, transcription initiation |
| marc024a_ct_mv | 10.1038/emboj.2010.266 |
| match_str | fernandeztornero2010conformationalflexibilityofrnapolymeraseiiiduringtranscriptionalelongation |
| mega_collection | Verbunddaten SWB, Lizenzfreie Online-Ressourcen |
| misc_de105 | EBOOK |
| multipart_link | 075961377 |
| multipart_part | (075961377)29(2010), 22, Seite 3762-3772 |
| names_id_str_mv | (DE-588)1132163307, (DE-627)887456839, (DE-576)488671744, (DE-588)1038353319, (DE-627)766122247, (DE-576)392341069 |
| oclc_num | 1340975466 |
| physical | 11 |
| publishDate | 22 October 2010 |
| publishDateSort | 2010 |
| publishPlace | |
| publisher | |
| record_format | marcfinc |
| record_id | 488671655 |
| recordtype | marcfinc |
| rvk_facet | No subject assigned |
| source_id | 0 |
| spelling | Fernández‐Tornero, Carlos VerfasserIn (DE-588)1132163307 (DE-627)887456839 (DE-576)488671744 aut, Conformational flexibility of RNA polymerase III during transcriptional elongation Carlos Fernández‐Tornero, Bettina Böttcher, Umar Jan Rashid, Ulrich Steuerwald, Beate Flörchinger, Damien P. Devos, Doris Lindner and Christoph W. Müller, 22 October 2010, 11, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Gesehen am 16.05.2017, RNA polymerase (Pol) III is responsible for the transcription of genes encoding small RNAs, including tRNA, 5S rRNA and U6 RNA. Here, we report the electron cryomicroscopy structures of yeast Pol III at 9.9 Å resolution and its elongation complex at 16.5 Å resolution. Particle sub‐classification reveals prominent EM densities for the two Pol III‐specific subcomplexes, C31/C82/C34 and C37/C53, that can be interpreted using homology models. While the winged‐helix‐containing C31/C82/C34 subcomplex initiates transcription from one side of the DNA‐binding cleft, the C37/C53 subcomplex accesses the transcription bubble from the opposite side of this cleft. The transcribing Pol III enzyme structure not only shows the complete incoming DNA duplex, but also reveals the exit path of newly synthesized RNA. During transcriptional elongation, the Pol III‐specific subcomplexes tightly enclose the incoming DNA duplex, which likely increases processivity and provides structural insights into the conformational switch between Pol III‐mediated initiation and elongation., electron cryomicroscopy, elongation complex, RNA polymerase III, transcription elongation, transcription initiation, Devos, Damien VerfasserIn (DE-588)1038353319 (DE-627)766122247 (DE-576)392341069 aut, Enthalten in European Molecular Biology Organization The EMBO journal Heidelberg : EMBO Press, 1982 29(2010), 22, Seite 3762-3772 (DE-627)266022529 (DE-600)1467419-1 (DE-576)075961377 1460-2075 nnns, volume:29 year:2010 number:22 pages:3762-3772 extent:11, http://dx.doi.org/10.1038/emboj.2010.266 Verlag Resolving-System kostenfrei Volltext, http://emboj.embopress.org/content/29/22/3762 Verlag kostenfrei Volltext, http://dx.doi.org/10.1038/emboj.2010.266 LFER, LFER 2017-06-08T00:00:00Z |
| spellingShingle | Fernández‐Tornero, Carlos, Devos, Damien, Conformational flexibility of RNA polymerase III during transcriptional elongation, RNA polymerase (Pol) III is responsible for the transcription of genes encoding small RNAs, including tRNA, 5S rRNA and U6 RNA. Here, we report the electron cryomicroscopy structures of yeast Pol III at 9.9 Å resolution and its elongation complex at 16.5 Å resolution. Particle sub‐classification reveals prominent EM densities for the two Pol III‐specific subcomplexes, C31/C82/C34 and C37/C53, that can be interpreted using homology models. While the winged‐helix‐containing C31/C82/C34 subcomplex initiates transcription from one side of the DNA‐binding cleft, the C37/C53 subcomplex accesses the transcription bubble from the opposite side of this cleft. The transcribing Pol III enzyme structure not only shows the complete incoming DNA duplex, but also reveals the exit path of newly synthesized RNA. During transcriptional elongation, the Pol III‐specific subcomplexes tightly enclose the incoming DNA duplex, which likely increases processivity and provides structural insights into the conformational switch between Pol III‐mediated initiation and elongation., electron cryomicroscopy, elongation complex, RNA polymerase III, transcription elongation, transcription initiation |
| swb_id_str | 488671655 |
| title | Conformational flexibility of RNA polymerase III during transcriptional elongation |
| title_auth | Conformational flexibility of RNA polymerase III during transcriptional elongation |
| title_full | Conformational flexibility of RNA polymerase III during transcriptional elongation Carlos Fernández‐Tornero, Bettina Böttcher, Umar Jan Rashid, Ulrich Steuerwald, Beate Flörchinger, Damien P. Devos, Doris Lindner and Christoph W. Müller |
| title_fullStr | Conformational flexibility of RNA polymerase III during transcriptional elongation Carlos Fernández‐Tornero, Bettina Böttcher, Umar Jan Rashid, Ulrich Steuerwald, Beate Flörchinger, Damien P. Devos, Doris Lindner and Christoph W. Müller |
| title_full_unstemmed | Conformational flexibility of RNA polymerase III during transcriptional elongation Carlos Fernández‐Tornero, Bettina Böttcher, Umar Jan Rashid, Ulrich Steuerwald, Beate Flörchinger, Damien P. Devos, Doris Lindner and Christoph W. Müller |
| title_in_hierarchy | Conformational flexibility of RNA polymerase III during transcriptional elongation / Carlos Fernández‐Tornero, Bettina Böttcher, Umar Jan Rashid, Ulrich Steuerwald, Beate Flörchinger, Damien P. Devos, Doris Lindner and Christoph W. Müller, |
| title_short | Conformational flexibility of RNA polymerase III during transcriptional elongation |
| title_sort | conformational flexibility of rna polymerase iii during transcriptional elongation |
| topic | electron cryomicroscopy, elongation complex, RNA polymerase III, transcription elongation, transcription initiation |
| topic_facet | electron cryomicroscopy, elongation complex, RNA polymerase III, transcription elongation, transcription initiation |
| url | http://dx.doi.org/10.1038/emboj.2010.266, http://emboj.embopress.org/content/29/22/3762 |