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A mechanism for all polymerases

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  • Thomas A. Steitz

    (Yale University)

Abstract

Replication of the genome is one of the most fundamental of biological activities, hence the interest in the mechanism by which the enzymes concerned -- the polynucleotide polymerases -- carry out the process. The co-crystal structures of the DNA polymerase that replicates bacteriophage T7, and of theBacillus stearothermophilusDNA polymerase large fragment, provide significant insights into the catalytic mechanism, fidelity and processivity of DNA polymerases.

Suggested Citation

  • Thomas A. Steitz, 1998. "A mechanism for all polymerases," Nature, Nature, vol. 391(6664), pages 231-232, January.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6664:d:10.1038_34542
    DOI: 10.1038/34542
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    Cited by:

    1. Alec Fraser & Maria L. Sokolova & Arina V. Drobysheva & Julia V. Gordeeva & Sergei Borukhov & John Jumper & Konstantin V. Severinov & Petr G. Leiman, 2022. "Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Chia-Shin Yang & Tzu-Ping Ko & Chao-Jung Chen & Mei-Hui Hou & Yu-Chuan Wang & Yeh Chen, 2023. "Crystal structure and functional implications of cyclic di-pyrimidine-synthesizing cGAS/DncV-like nucleotidyltransferases," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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