Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-10-30
pubmed:databankReference
pubmed:abstractText
A DNA library of strain HB19 from Borrelia burgdorferi sensu stricto, an agent of Lyme borreliosis, was constructed in the cosmid pLA2917. Genes involved in initiation of DNA replication and resolution of recombination intermediates (Holliday junctions) were found on a 23-kbp region up to 0.7 kbp of the "left" extremity of the linear chromosome in representative species of B. burgdorferi sensu lato. The potential ruvB gene, located at 22 kbp from the left telomere, was identified by the similarity of its deduced amino acid sequence to RuvB (helicases) of other bacteria. B. burgdorferi ruvB is part of an operon which comprises the homologues of ruvA, queA and pfbB. Expression of the B. burgdorferi ruvB and ruvA genes renders a wild-type Escherichia coli sensitive to UV light and mitomycin, indicative of negative complementation. priA, which encodes the potential recognition factor for the primosome assembly site, was found at 15 kbp from the left telomere. RuvB and PriA sequences have motifs characteristic of helicases: a DExH box and an ATP binding site.
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, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Holliday junction DNA helicase, E..., http://linkedlifedata.com/resource/pubmed/chemical/Intramolecular Transferases, http://linkedlifedata.com/resource/pubmed/chemical/Isomerases, http://linkedlifedata.com/resource/pubmed/chemical/Pentosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases, http://linkedlifedata.com/resource/pubmed/chemical/RuvB protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/S-adenosylmethionine - tRNA..., http://linkedlifedata.com/resource/pubmed/chemical/priA protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/pyrophosphate-fructose 6-phosphate..., http://linkedlifedata.com/resource/pubmed/chemical/tRNA-pseudouridine synthase I
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0923-2508
pubmed:author
pubmed:issnType
Print
pubmed:volume
149
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
235-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9766225-Adenosine Triphosphatases, pubmed-meshheading:9766225-Amino Acid Sequence, pubmed-meshheading:9766225-Bacterial Proteins, pubmed-meshheading:9766225-Borrelia burgdorferi Group, pubmed-meshheading:9766225-Cosmids, pubmed-meshheading:9766225-DNA, Bacterial, pubmed-meshheading:9766225-DNA Helicases, pubmed-meshheading:9766225-DNA Repair, pubmed-meshheading:9766225-DNA Replication, pubmed-meshheading:9766225-DNA-Binding Proteins, pubmed-meshheading:9766225-Escherichia coli Proteins, pubmed-meshheading:9766225-Intramolecular Transferases, pubmed-meshheading:9766225-Isomerases, pubmed-meshheading:9766225-Lyme Disease, pubmed-meshheading:9766225-Molecular Sequence Data, pubmed-meshheading:9766225-Pentosyltransferases, pubmed-meshheading:9766225-Phosphotransferases, pubmed-meshheading:9766225-Sequence Alignment, pubmed-meshheading:9766225-Transcription, Genetic
pubmed:year
1998
pubmed:articleTitle
Homologues of helicase genes priA and ruvAB of Borrelia burgdorferi, the Lyme borreliosis agent.
pubmed:affiliation
Unité de Bactériologie Moléculaire et Médicale, Institut Pasteur, Paris.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't