A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference32 articles.
1. Bacteriophage T7: Minimal requirements for the replication of a duplex DNA molecule
2. Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7.
3. An N-terminal fragment of the gene 4 helicase/primase of bacteriophage T7 retains primase activity in the absence of helicase activity
4. The Linker Region between the Helicase and Primase Domains of the Bacteriophage T7 Gene 4 Protein Is Critical for Hexamer Formation
5. Purification and characterization of the bacteriophage T7 gene 2.5 protein. A single-stranded DNA-binding protein.
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1. Mapping fast DNA polymerase exchange during replication;Nature Communications;2024-06-22
2. Regulation of T7 gp2.5 binding dynamics by its C-terminal tail, template conformation and sequence;Nucleic Acids Research;2023-05-31
3. From Processivity to Genome Maintenance: The Many Roles of Sliding Clamps;Genes;2022-11-07
4. Real-time label-free assessment of T7 DNA polymerase immobilization;Materials Today Nano;2022-08
5. Residues located in the primase domain of the bacteriophage T7 primase-helicase are essential for loading the hexameric complex onto DNA;Journal of Biological Chemistry;2022-06
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