title: Hairpin telomeres and genome plasticity in Borrelia: all mixed up in the end.
abstract: Spirochetes of the genus Borrelia have a highly unusual genome structure composed of over 20 replicons. Most of these replicons are linear and terminated by covalently closed hairpin ends or telomeres. Moreover, the linear replicons are affected by extensive DNA rearrangements, including telomere exchanges, DNA duplications, and harbour a large number of pseudogenes. The mechanism for the unusual genome plasticity in the linear replicons has remained elusive. The enzymatic machinery (the telomere resolvase ResT) responsible for generating the hairpin ends from replicative intermediates has recently been shown to also perform a reverse reaction that fuses telomeres on unrelated replicons. Infrequent stabilization of such fusion events over evolutionary time provides the first proposed biochemical mechanism for the DNA rearrangements that are so prominent in the linear replicons of B. burgdorferi.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta T2N 4N1, Canada. chaconas@ucalgary.ca
authors.forename: George
authors.initials: G
authors.lastname: Chaconas
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D025065:Borrelia burgdorferi / Q000235:genetics* / Q000378:metabolism; D002876:Chromosomes, Bacterial; D004706:Endodeoxyribonucleases / Q000378:metabolism; D015321:Gene Rearrangement; D016680:Genome, Bacterial; D009690:Nucleic Acid Conformation; D011995:Recombination, Genetic; D012093:Replicon; D016615:Telomere / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D004706:Endodeoxyribonucleases; C446515:ResT protein, Borrelia