PMID:16469698: Difference between revisions
imported>Wikientrybot Fix links due to TableEditLinks.php changes. |
imported>Wikientrybot change PMID template to TableEdit version |
||
| (4 intermediate revisions by 2 users not shown) | |||
| Line 1: | Line 1: | ||
{{RightTOC}} | {{RightTOC}} | ||
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.114437.D52238ccd091c3--> | |||
<!-- | |||
****************************************************************************************** | |||
* | |||
* ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | |||
* | |||
****************************************************************************************** --> | |||
{| id="D52238ccd091c3" class=" tableEdit PMID_info_table" | |||
|- | |- | ||
| | !align=left |Citation | ||
|| | |||
'''Deaconescu, AM, Chambers, AL, Smith, AJ, Nickels, BE, Hochschild, A, Savery, NJ and Darst, SA''' (2006) Structural basis for bacterial transcription-coupled DNA repair. ''Cell'' '''124''':507-20 | |||
|- | |||
!align=left |Abstract | |||
|| | |||
Coupling of transcription and DNA repair in bacteria is mediated by transcription-repair coupling factor (TRCF, the product of the mfd gene), which removes transcription elongation complexes stalled at DNA lesions and recruits the nucleotide excision repair machinery to the site. Here we describe the 3.2 A-resolution X-ray crystal structure of Escherichia coli TRCF. The structure consists of a compact arrangement of eight domains, including a translocation module similar to the SF2 ATPase RecG, and a region of structural similarity to UvrB. Biochemical and genetic experiments establish that another domain with structural similarity to the Tudor-like domain of the transcription elongation factor NusG plays a critical role in TRCF/RNA polymerase interactions. Comparison with the translocation module of RecG as well as other structural features indicate that TRCF function involves large-scale conformational changes. These data, along with a structural model for the interaction of TRCF with the transcription elongation complex, provide mechanistic insights into TRCF function. | |||
|- | |||
!align=left |Links | |||
|| | |||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16469698 PubMed] | |||
Online version:[http://dx.doi.org/10.1016/j.cell.2005.11.045 10.1016/j.cell.2005.11.045] | |||
|- | |- | ||
|{{ | !align=left |Keywords | ||
|| | |||
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Crystallography, X-Ray; DNA Helicases/chemistry; DNA Helicases/genetics; DNA Helicases/metabolism; DNA Repair; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Transcription Factors/chemistry; Transcription Factors/genetics; Transcription Factors/metabolism; Transcription, Genetic | |||
|- class="tableEdit_footer" | |||
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.114437.D52238ccd091c3&page=114437&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> || | |||
|} | |} | ||
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.114437.D52238ccd091c3--> | |||
==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
| Line 18: | Line 38: | ||
==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
< | <annotationlinks/> | ||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:29, 15 September 2013
| Citation |
Deaconescu, AM, Chambers, AL, Smith, AJ, Nickels, BE, Hochschild, A, Savery, NJ and Darst, SA (2006) Structural basis for bacterial transcription-coupled DNA repair. Cell 124:507-20 |
|---|---|
| Abstract |
Coupling of transcription and DNA repair in bacteria is mediated by transcription-repair coupling factor (TRCF, the product of the mfd gene), which removes transcription elongation complexes stalled at DNA lesions and recruits the nucleotide excision repair machinery to the site. Here we describe the 3.2 A-resolution X-ray crystal structure of Escherichia coli TRCF. The structure consists of a compact arrangement of eight domains, including a translocation module similar to the SF2 ATPase RecG, and a region of structural similarity to UvrB. Biochemical and genetic experiments establish that another domain with structural similarity to the Tudor-like domain of the transcription elongation factor NusG plays a critical role in TRCF/RNA polymerase interactions. Comparison with the translocation module of RecG as well as other structural features indicate that TRCF function involves large-scale conformational changes. These data, along with a structural model for the interaction of TRCF with the transcription elongation complex, provide mechanistic insights into TRCF function. |
| Links |
PubMed Online version:10.1016/j.cell.2005.11.045 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Crystallography, X-Ray; DNA Helicases/chemistry; DNA Helicases/genetics; DNA Helicases/metabolism; DNA Repair; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Transcription Factors/chemistry; Transcription Factors/genetics; Transcription Factors/metabolism; Transcription, Genetic |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.