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PMID: 2530914 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A general method of site-specific mutagenesis using a modification of the Thermus aquaticus polymerase chain reaction.

Analytical biochemistry ·Vol. 180 ·No. 1 ·1989-07-00 ·Pages 147-51

Nelson RM, Long GL

Abstract

A specific mutagenic change in the cDNA of human protein S was introduced by a modification of the polymerase chain reaction that permits the introduction of a mutation at any position in a double-stranded DNA molecule. The method employed four synthetic oligonucleotide primers. One oligonucleotide contained a single-base mismatch to direct the mutagenesis; the other three oligonucleotides were designed to allow selective amplification of the mutated sequence with Thermus aquaticus polymerase. The mutagenized cDNA was cloned into a plasmid vector and transformed into Escherichia coli RR1 cells for characterization. The desired cytosine to guanine change in the target cDNA was confirmed by the predicted appearance of an AluI restriction site and by dideoxynucleotide sequencing. No other sequence changes were detected within the amplified region. This method of site-specific mutagenesis can be applied to any linear double-stranded DNA large enough for primer annealing and obviates specialized cloning vectors, DNA constructs, and selection techniques. It has the advantage over a recently published PCR technique (R. Higuchi, B. Krummel, and R. Saki (1988) Nucleic Acids Res. 16, 7351-7367) in requiring no diafiltration to remove primers between steps and in requiring only a single mutagenic oligonucleotide to be synthesized for each mutant construct made after the initial one.

MeSH Terms
Base Sequence DNA Mutational Analysis DNA-Directed DNA Polymerase Escherichia coli/genetics Glycoproteins/genetics Humans Nucleic Acid Amplification Techniques Plasmids Polymerase Chain Reaction/methods Protein S Taq Polymerase Thermus/enzymology Transformation, Genetic
Chemicals
Glycoproteins Protein S Taq Polymerase DNA-Directed DNA Polymerase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Nelson R M
Department of Biochemistry, University of Vermont College of Medicine, Burlington 05405.
Long G L
Article Info
Journal
Analytical biochemistry
Abbr.
Anal Biochem
ISSN
0003-2697
Published
1989-07-00
Pages
147-51
Language
English
Region
United States
NLM ID
0370535
Subset
IM
Grants
NHLBI NIH HHS · C06 HL39745 · United States
NHLBI NIH HHS · R01 HL38899 · United States
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