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Title: High processivity polymerases

Abstract

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.

Inventors:
;
Publication Date:
Research Org.:
William Marsh Rice University, Houston, TX (USA)
Sponsoring Org.:
USDOE
OSTI Identifier:
1134259
Patent Number(s):
8,748,147
Application Number:
11/945,877
Assignee:
William Marsh Rice University (Houston, TX)
DOE Contract Number:  
W-31-109-ENG-38
Resource Type:
Patent
Resource Relation:
Patent File Date: 2007 Nov 27
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Shamoo, Yousif, and Sun, Siyang. High processivity polymerases. United States: N. p., 2014. Web.
Shamoo, Yousif, & Sun, Siyang. High processivity polymerases. United States.
Shamoo, Yousif, and Sun, Siyang. 2014. "High processivity polymerases". United States. https://www.osti.gov/servlets/purl/1134259.
@article{osti_1134259,
title = {High processivity polymerases},
author = {Shamoo, Yousif and Sun, Siyang},
abstractNote = {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.},
doi = {},
url = {https://www.osti.gov/biblio/1134259}, journal = {},
number = ,
volume = ,
place = {United States},
year = {Tue Jun 10 00:00:00 EDT 2014},
month = {Tue Jun 10 00:00:00 EDT 2014}
}

Works referenced in this record:

Nucleic acid modifying enzymes
patent, June 2009


Single stranded DNA binding proteins from Archaea and uses therefor
patent, February 2010


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