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| | ==Solution Structure of RfaH carboxyterminal domain== | | ==Solution Structure of RfaH carboxyterminal domain== |
| - | <StructureSection load='2lcl' size='340' side='right'caption='[[2lcl]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lcl' size='340' side='right'caption='[[2lcl]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lcl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LCL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lcl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LCL FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rfaH, hlyT, sfrB, Z5362, ECs4770 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lcl OCA], [https://pdbe.org/2lcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lcl RCSB], [https://www.ebi.ac.uk/pdbsum/2lcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lcl ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lcl OCA], [https://pdbe.org/2lcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lcl RCSB], [https://www.ebi.ac.uk/pdbsum/2lcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lcl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RFAH_ECO57 RFAH_ECO57]] Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components. RfaH is recruited into a multi-component RNA polymerase complex by the ops element, which is a short conserved DNA sequence located downstream of the main promoter of these operons. Once bound, RfaH suppresses pausing and inhibits Rho-dependent and intrinsic termination at a subset of sites. Termination signals are bypassed, which allows complete synthesis of long RNA chains.
| + | [https://www.uniprot.org/uniprot/RFAH_ECO57 RFAH_ECO57] Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components. RfaH is recruited into a multi-component RNA polymerase complex by the ops element, which is a short conserved DNA sequence located downstream of the main promoter of these operons. Once bound, RfaH suppresses pausing and inhibits Rho-dependent and intrinsic termination at a subset of sites. Termination signals are bypassed, which allows complete synthesis of long RNA chains. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco57]] | + | [[Category: Escherichia coli O157:H7]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Burmann, B M]] | + | [[Category: Burmann BM]] |
| - | [[Category: Roesch, P]] | + | [[Category: Roesch P]] |
| - | [[Category: Schweimer, K]] | + | [[Category: Schweimer K]] |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription antitermination]]
| + | |
| - | [[Category: Transcription elongation]]
| + | |
| - | [[Category: Transcription pausing]]
| + | |
| Structural highlights
Function
RFAH_ECO57 Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components. RfaH is recruited into a multi-component RNA polymerase complex by the ops element, which is a short conserved DNA sequence located downstream of the main promoter of these operons. Once bound, RfaH suppresses pausing and inhibits Rho-dependent and intrinsic termination at a subset of sites. Termination signals are bypassed, which allows complete synthesis of long RNA chains.
Publication Abstract from PubMed
NusG homologs regulate transcription and coupled processes in all living organisms. The Escherichia coli (E. coli) two-domain paralogs NusG and RfaH have conformationally identical N-terminal domains (NTDs) but dramatically different carboxy-terminal domains (CTDs), a beta barrel in NusG and an alpha hairpin in RfaH. Both NTDs interact with elongating RNA polymerase (RNAP) to reduce pausing. In NusG, NTD and CTD are completely independent, and NusG-CTD interacts with termination factor Rho or ribosomal protein S10. In contrast, RfaH-CTD makes extensive contacts with RfaH-NTD to mask an RNAP-binding site therein. Upon RfaH interaction with its DNA target, the operon polarity suppressor (ops) DNA, RfaH-CTD is released, allowing RfaH-NTD to bind to RNAP. Here, we show that the released RfaH-CTD completely refolds from an all-alpha to an all-beta conformation identical to that of NusG-CTD. As a consequence, RfaH-CTD binding to S10 is enabled and translation of RfaH-controlled operons is strongly potentiated. PAPERFLICK:
An alpha helix to beta barrel domain switch transforms the transcription factor RfaH into a translation factor.,Burmann BM, Knauer SH, Sevostyanova A, Schweimer K, Mooney RA, Landick R, Artsimovitch I, Rosch P Cell. 2012 Jul 20;150(2):291-303. doi: 10.1016/j.cell.2012.05.042. PMID:22817892[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Burmann BM, Knauer SH, Sevostyanova A, Schweimer K, Mooney RA, Landick R, Artsimovitch I, Rosch P. An alpha helix to beta barrel domain switch transforms the transcription factor RfaH into a translation factor. Cell. 2012 Jul 20;150(2):291-303. doi: 10.1016/j.cell.2012.05.042. PMID:22817892 doi:http://dx.doi.org/10.1016/j.cell.2012.05.042
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