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TWINKLE Has 5' -> 3' DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein.

Artikel i vetenskaplig tidskrift
Författare Jenny A Korhonen
Martina Gaspari
Maria Falkenberg
Publicerad i The Journal of biological chemistry
Volym 278
Nummer/häfte 49
Sidor 48627-32
ISSN 0021-9258
Publiceringsår 2003
Publicerad vid
Sidor 48627-32
Språk en
Ämnesord Animals, Base Sequence, Cell Line, DNA Helicases, metabolism, DNA Primase, metabolism, DNA Primers, DNA-Binding Proteins, metabolism, Mitochondria, metabolism, Recombinant Proteins, metabolism
Ämneskategorier Kemi

Sammanfattning

Mutations in TWINKLE cause autosomal dominant progressive external ophthalmoplegia, a human disorder associated with multiple deletions in the mitochondrial DNA. TWINKLE displays primary sequence similarity to the phage T7 gene 4 primase-helicase, but no specific enzyme activity has been assigned to the protein. We have purified recombinant TWINKLE to near homogeneity and demonstrate here that TWINKLE is a DNA helicase with 5' to 3' directionality and distinct substrate requirements. The protein needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. The helicase activity has an absolute requirement for hydrolysis of a nucleoside 5'-triphosphate, with UTP being the optimal substrate. DNA unwinding by TWINKLE is specifically stimulated by the mitochondrial single-stranded DNA-binding protein. Our enzymatic characterization strongly supports the notion that TWINKLE is the helicase at the mitochondrial DNA replication fork and provides evidence for a close relationship of the DNA replication machinery in bacteriophages and mammalian mitochondria.

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