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.
© The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.
Publication types
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Research Support, N.I.H., Intramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Basic-Leucine Zipper Transcription Factors / chemistry
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Basic-Leucine Zipper Transcription Factors / genetics
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Basic-Leucine Zipper Transcription Factors / metabolism*
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DNA Helicases / chemistry
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DNA Helicases / genetics
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DNA Helicases / metabolism*
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DNA Replication
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DNA, Single-Stranded / chemistry
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DNA, Single-Stranded / genetics
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Exodeoxyribonucleases / chemistry
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Exodeoxyribonucleases / genetics
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Exodeoxyribonucleases / metabolism*
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Fanconi Anemia Complementation Group Proteins / chemistry
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Fanconi Anemia Complementation Group Proteins / genetics
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Fanconi Anemia Complementation Group Proteins / metabolism*
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G-Quadruplexes*
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Gene Expression
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Guanine / chemistry
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Guanine / metabolism
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Humans
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RecQ Helicases / chemistry
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RecQ Helicases / genetics
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RecQ Helicases / metabolism*
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Werner Syndrome Helicase
Substances
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BACH1 protein, human
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Basic-Leucine Zipper Transcription Factors
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DNA, Single-Stranded
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Fanconi Anemia Complementation Group Proteins
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Guanine
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Exodeoxyribonucleases
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RTEL1 protein, human
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DNA Helicases
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DNA2 protein, human
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RecQ Helicases
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WRN protein, human
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Werner Syndrome Helicase
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PIF1 protein, human