title: G-quadruplexes and helicases.
abstract: Guanine-rich DNA strands can fold in vitro into non-canonical DNA structures called G-quadruplexes. These structures may be very stable under physiological conditions. Evidence suggests that G-quadruplex structures may act as 'knots' within genomic DNA, and it has been hypothesized that proteins may have evolved to remove these structures. The first indication of how G-quadruplex structures could be unfolded enzymatically came in the late 1990s with reports that some well-known duplex DNA helicases resolved these structures in vitro. Since then, the number of studies reporting G-quadruplex DNA unfolding by helicase enzymes has rapidly increased. The present review aims to present a general overview of the helicase/G-quadruplex field.
authors.affiliation: University of Bordeaux, ARNA Laboratory F-33000 Bordeaux, France INSERM U1212,CNRS UMR 5320, IECB, F-33600 Pessac, France.
authors.forename: Oscar
authors.initials: O
authors.lastname: Mendoza
authors.affiliation: University of Bordeaux, ARNA Laboratory F-33000 Bordeaux, France INSERM U1212,CNRS UMR 5320, IECB, F-33600 Pessac, France.
authors.forename: Anne
authors.initials: A
authors.lastname: Bourdoncle
authors.affiliation: CNRS UMR 7196, INSERM U1154, MNHN, F-75005 Paris, France Sorbonne Universités, F-75005 Paris, France jean-baptiste.boule@mnhn.fr.
authors.forename: Jean-Baptiste
authors.initials: JB
authors.lastname: Boulé
authors.affiliation: Laboratory of Molecular Gerontology, National Institute on Aging, NIH, Baltimore, MD 21224, USA broshr@grc.nia.nih.gov.
authors.forename: Robert M
authors.initials: RM
authors.lastname: Brosh
authors.affiliation: University of Bordeaux, ARNA Laboratory F-33000 Bordeaux, France INSERM U1212,CNRS UMR 5320, IECB, F-33600 Pessac, France jean-louis.mergny@inserm.fr.
authors.forename: Jean-Louis
authors.initials: JL
authors.lastname: Mergny
mesh_terms: D050976:Basic-Leucine Zipper Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004265:DNA Helicases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004261:DNA Replication; D004277:DNA, Single-Stranded / Q000737:chemistry / Q000235:genetics; D005090:Exodeoxyribonucleases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051856:Fanconi Anemia Complementation Group Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D054856:G-Quadruplexes; D015870:Gene Expression; D006147:Guanine / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D053484:RecQ Helicases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000071657:Werner Syndrome Helicase
chemical_list: C102108:BACH1 protein, human; D050976:Basic-Leucine Zipper Transcription Factors; D004277:DNA, Single-Stranded; D051856:Fanconi Anemia Complementation Group Proteins; D006147:Guanine; D005090:Exodeoxyribonucleases; C532890:RTEL1 protein, human; D004265:DNA Helicases; C509908:DNA2 protein, human; D053484:RecQ Helicases; C098785:WRN protein, human; D000071657:Werner Syndrome Helicase; C508765:PIF1 protein, human