High processivity polymerases
Patent
·
OSTI ID:1134259
Chimeric proteins comprising a sequence nonspecific single-stranded nucleic-acid-binding domain joined to a catalytic nucleic-acid-modifying domain are provided. Methods comprising contacting a nucleic acid molecule with a chimeric protein, as well as systems comprising a nucleic acid molecule, a chimeric protein, and an aqueous solution are also provided. The joining of sequence nonspecific single-stranded nucleic-acid-binding domain and a catalytic nucleic-acid-modifying domain in chimeric proteins, among other things, may prevent the separation of the two domains due to their weak association and thereby enhances processivity while maintaining fidelity.
- Research Organization:
- William Marsh Rice University, Houston, TX (USA)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- W-31109-ENG-38
- Assignee:
- William Marsh Rice University (Houston, TX)
- Patent Number(s):
- 8,748,147
- Application Number:
- 11/945,877
- OSTI ID:
- 1134259
- Country of Publication:
- United States
- Language:
- English
Modular Organization of T4 DNA Polymerase: EVIDENCE FROM PHYLOGENETICS
|
journal | November 1995 |
Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity
|
journal | July 2006 |
Divergence of the mRNA targets for the Ssb proteins of bacteriophages T4 and RB69
|
journal | January 2004 |
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