PMID:8465200: Difference between revisions
Fill PMID: Page! |
imported>Wikientrybot change PMID template to TableEdit version |
||
| Line 1: | Line 1: | ||
{{RightTOC}} | {{RightTOC}} | ||
< | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.171947.J522399e50a471--> | ||
< | <!-- | ||
****************************************************************************************** | |||
* | |||
* ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | |||
* | |||
****************************************************************************************** --> | |||
{| id="J522399e50a471" class=" tableEdit PMID_info_table" | |||
|- | |- | ||
| | !align=left |Citation | ||
|| | |||
'''No author listed''' (1993) Molecular mechanism of transcription-repair coupling. ''Science'' '''260''':53-8 | |||
|- | |- | ||
| | !align=left |Abstract | ||
|| | |||
Lesions in the transcribed strand block transcription and are repaired more rapidly than lesions in the nontranscribed (coding) strand which do not block RNA polymerase (RNAP). It has been shown previously that in Escherichia coli the mfd (mutation frequency decline) gene is necessary for strand-specific repair. The mfd gene was cloned and sequenced and the Mfd protein was purified and used to reconstitute strand-specific repair in a completely defined system. The mfd gene encodes a protein of 130 kilodaltons and contains the so-called "helicase motifs," a leucine zipper motif, and regions of sequence similarity to UvrB and RecG proteins. The Mfd protein was shown to (i) displace RNAP stalled at a lesion in an adenosine triphosphate-dependent reaction, (ii) bind to the damage recognition subunit (UvrA) of the excision nuclease, and (iii) stimulate the repair of the transcribed strand only when transcription is taking place. Thus, Mfd appears to target the transcribed strand for repair by recognizing a stalled RNAP and actively recruiting the repair enzyme to the transcription blocking lesion as it dissociates the stalled RNAP. | |||
|- | |||
!align=left |Links | |||
|| | |||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8465200 PubMed] | |||
|- | |||
!align=left |Keywords | |||
|| | |||
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Binding Sites; Cloning, Molecular; DNA Helicases; DNA Repair/genetics; DNA, Bacterial/metabolism; DNA-Directed RNA Polymerases/metabolism; Endodeoxyribonucleases/metabolism; Escherichia coli/genetics; Escherichia coli Proteins; Leucine Zippers; Molecular Sequence Data; Multienzyme Complexes/chemistry; Multienzyme Complexes/genetics; Mutation/genetics; 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.171947.J522399e50a471&page=171947&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> || | |||
|} | |} | ||
< | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.171947.J522399e50a471--> | ||
==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
Revision as of 19:47, 1 September 2013
| Citation |
No author listed (1993) Molecular mechanism of transcription-repair coupling. Science 260:53-8 |
|---|---|
| Abstract |
Lesions in the transcribed strand block transcription and are repaired more rapidly than lesions in the nontranscribed (coding) strand which do not block RNA polymerase (RNAP). It has been shown previously that in Escherichia coli the mfd (mutation frequency decline) gene is necessary for strand-specific repair. The mfd gene was cloned and sequenced and the Mfd protein was purified and used to reconstitute strand-specific repair in a completely defined system. The mfd gene encodes a protein of 130 kilodaltons and contains the so-called "helicase motifs," a leucine zipper motif, and regions of sequence similarity to UvrB and RecG proteins. The Mfd protein was shown to (i) displace RNAP stalled at a lesion in an adenosine triphosphate-dependent reaction, (ii) bind to the damage recognition subunit (UvrA) of the excision nuclease, and (iii) stimulate the repair of the transcribed strand only when transcription is taking place. Thus, Mfd appears to target the transcribed strand for repair by recognizing a stalled RNAP and actively recruiting the repair enzyme to the transcription blocking lesion as it dissociates the stalled RNAP. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Binding Sites; Cloning, Molecular; DNA Helicases; DNA Repair/genetics; DNA, Bacterial/metabolism; DNA-Directed RNA Polymerases/metabolism; Endodeoxyribonucleases/metabolism; Escherichia coli/genetics; Escherichia coli Proteins; Leucine Zippers; Molecular Sequence Data; Multienzyme Complexes/chemistry; Multienzyme Complexes/genetics; Mutation/genetics; 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
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| edit table |
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
See also
References
See Help:References for how to manage references in EcoliWiki.