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Title: 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-31-109-ENG-38
Assignee:
William Marsh Rice University (Houston, TX)
Patent Number(s):
8,748,147
Application Number:
11/945,877
OSTI ID:
1134259
Resource Relation:
Patent File Date: 2007 Nov 27
Country of Publication:
United States
Language:
English

References (7)

Nucleic acid modifying enzymes patent June 2009
Single stranded DNA binding proteins from Archaea and uses therefor patent February 2010
Method for increasing the processivity of a DNA- or RNA-dependent polymerase and compositions therefor patent-application August 2002
Methods of using improved polymerases patent-application January 2004
Divergence of the mRNA targets for the Ssb proteins of bacteriophages T4 and RB69 journal January 2004
Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity journal July 2006
Modular Organization of T4 DNA Polymerase: EVIDENCE FROM PHYLOGENETICS journal November 1995

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