Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-5-22
pubmed:abstractText
We have discovered a correlation between the ability of Escherichia coli cells to survive damage to DNA and their ability to modulate RNA polymerase via the stringent response regulators, (p)ppGpp. Elevation of (p)ppGpp, or certain mutations in the beta subunit of RNA polymerase, dramatically improve survival of UV-irradiated strains lacking the RuvABC Holliday junction resolvase. Increased survival depends on excision and recombination proteins and relies on the ability of RecG helicase to form Holliday junctions from replication forks stalled at lesions in the DNA and of PriA to initiate replication restart. The role of RecG provides novel insights into the interplay between transcription, replication, and recombination, and suggests a general model in which recombination underpins genome duplication in the face of frequent obstacles to replication fork progression.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases, http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonuclease V, http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Pentaphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Holliday Junction Resolvases, http://linkedlifedata.com/resource/pubmed/chemical/Holliday junction DNA helicase, E..., http://linkedlifedata.com/resource/pubmed/chemical/Rec A Recombinases, http://linkedlifedata.com/resource/pubmed/chemical/RecG protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Replication Protein A, http://linkedlifedata.com/resource/pubmed/chemical/RusA protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/RuvB protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/UvrA protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/ruvC protein, E coli
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
101
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10778854-Adenosine Triphosphatases, pubmed-meshheading:10778854-Bacterial Proteins, pubmed-meshheading:10778854-DNA Damage, pubmed-meshheading:10778854-DNA Helicases, pubmed-meshheading:10778854-DNA Repair, pubmed-meshheading:10778854-DNA Replication, pubmed-meshheading:10778854-DNA-Binding Proteins, pubmed-meshheading:10778854-DNA-Directed RNA Polymerases, pubmed-meshheading:10778854-Endodeoxyribonucleases, pubmed-meshheading:10778854-Enzyme Activation, pubmed-meshheading:10778854-Escherichia coli, pubmed-meshheading:10778854-Escherichia coli Proteins, pubmed-meshheading:10778854-Exodeoxyribonuclease V, pubmed-meshheading:10778854-Exodeoxyribonucleases, pubmed-meshheading:10778854-Gene Deletion, pubmed-meshheading:10778854-Guanosine Pentaphosphate, pubmed-meshheading:10778854-Holliday Junction Resolvases, pubmed-meshheading:10778854-Rec A Recombinases, pubmed-meshheading:10778854-Replication Protein A, pubmed-meshheading:10778854-Ultraviolet Rays
pubmed:year
2000
pubmed:articleTitle
Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression.
pubmed:affiliation
Institute of Genetics, University of Nottingham, Queen's Medical Centre, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't