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Title: DNA polymerase having modified nucleotide binding site for DNA sequencing

Abstract

Modified gene encoding a modified DNA polymerase wherein the modified polymerase incorporates dideoxynucleotides at least 20-fold better compared to the corresponding deoxynucleotides as compared with the corresponding naturally-occurring DNA polymerase.

Inventors:
 [1];  [2]
  1. Cambridge, MA
  2. Chestnut Hill, MA
Issue Date:
Research Org.:
Harvard University
OSTI Identifier:
870881
Patent Number(s):
5614365
Assignee:
President & Fellow of Harvard College (Cambridge, MA)
Patent Classifications (CPCs):
C - CHEMISTRY C12 - BIOCHEMISTRY C12N - MICROORGANISMS OR ENZYMES
C - CHEMISTRY C12 - BIOCHEMISTRY C12Q - MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS
DOE Contract Number:  
FG02-88ER60688
Resource Type:
Patent
Country of Publication:
United States
Language:
English
Subject:
dna; polymerase; modified; nucleotide; binding; site; sequencing; encoding; incorporates; dideoxynucleotides; 20-fold; compared; corresponding; deoxynucleotides; naturally-occurring; dna polymerase; binding site; dna sequencing; modified polymer; /435/530/999/

Citation Formats

Tabor, Stanley, and Richardson, Charles. DNA polymerase having modified nucleotide binding site for DNA sequencing. United States: N. p., 1997. Web.
Tabor, Stanley, & Richardson, Charles. DNA polymerase having modified nucleotide binding site for DNA sequencing. United States.
Tabor, Stanley, and Richardson, Charles. Wed . "DNA polymerase having modified nucleotide binding site for DNA sequencing". United States. https://www.osti.gov/servlets/purl/870881.
@article{osti_870881,
title = {DNA polymerase having modified nucleotide binding site for DNA sequencing},
author = {Tabor, Stanley and Richardson, Charles},
abstractNote = {Modified gene encoding a modified DNA polymerase wherein the modified polymerase incorporates dideoxynucleotides at least 20-fold better compared to the corresponding deoxynucleotides as compared with the corresponding naturally-occurring DNA polymerase.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Wed Jan 01 00:00:00 EST 1997},
month = {Wed Jan 01 00:00:00 EST 1997}
}

Works referenced in this record:

Compilation and alignment of DNA polymerase sequences
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Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism
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Mutants Affecting Nucleotide Recognition by T7 DNA Polymerase
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Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP
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Ordered Appearance of Zidovudine Resistance Mutations during Treatment of 18 Human Immunodeficiency Virus-Positive Subjects
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Bacteriophage T4 DNA polymerase mutations that confer sensitivity to the PPi analog phosphonoacetic acid
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DNA sequencing with chain-terminating inhibitors
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Role of lysine 758 of Escherichia coli DNA polymerase I as assessed by site-directed mutagenesis.
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Resistance to ddI and sensitivity to AZT induced by a mutation in HIV-1 reverse transcriptase
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Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate
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Fluorescence detection in automated DNA sequence analysis
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Isolation and characterization of a dideoxyguanosine triphosphate-resistant mutant of human immunodeficiency virus reverse transcriptase.
journal, December 1991


Optimization of Parameters in a DNA Sequenator Using Fluorescence Detection
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A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity
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Fifth mutation in human immunodeficiency virus type 1 reverse transcriptase contributes to the development of high-level resistance to zidovudine.
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Related functional domains in virus DNA polymerases.
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Side chains involved in catalysis of the polymerase reaction of DNA polymerase I from Escherichia coli.
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A system for rapid DNA sequencing with fluorescent chain-terminating dideoxynucleotides
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Function and Structure Relationships in DNA Polymerases
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Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli.
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Identification of amino acids in herpes simplex virus DNA polymerase involved in substrate and drug recognition.
journal, September 1988