The N-terminal domain of human mitochondrial helicase Twinkle has DNA-binding activity crucial for supporting processive DNA synthesis by polymerase Î³.

Johnson, Laura C; Singh, Anupam; Patel, Smita S

Johnson, Laura C; Singh, Anupam; Patel, Smita S.

Afiliación

Johnson LC; Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers University, Piscataway, New Jersey, USA; Graduate School of Biomedical Sciences, Robert Wood Johnson Medical School, Rutgers University, Piscataway, New Jersey, USA.
Singh A; Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers University, Piscataway, New Jersey, USA.
Patel SS; Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers University, Piscataway, New Jersey, USA. Electronic address: patelss@rutgers.edu.

J Biol Chem ; 299(1): 102797, 2023 01.

Article en En | MEDLINE | ID: mdl-36528058

Asunto(s)

ADN Helicasas; Proteínas Mitocondriales; Humanos; ADN/metabolismo; ADN Helicasas/metabolismo; ADN Primasa/genética; ADN Primasa/metabolismo; Replicación del ADN; ADN Mitocondrial/metabolismo; Mitocondrias/genética; Mitocondrias/metabolismo; Proteínas Mitocondriales/metabolismo

Palabras clave

DNA polymerase; Twinkle; helicase; mitochondria; mitochondrial diseases; replication; replisome

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: ADN Helicasas / Proteínas Mitocondriales Límite: Humans Idioma: En Revista: J Biol Chem Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos

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