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PMID: 3151018 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A new method for random mutagenesis of complete genes: enzymatic generation of mutant libraries in vitro.

Protein engineering ·Vol. 2 ·No. 1 ·1988-04-00 ·Pages 63-8

Lehtovaara PM, Koivula AK, Bamford J, Knowles JK

Abstract

A new efficient in vitro mutagenesis method for the generation of complete random mutant libraries, containing all possible single base substitution mutations in a cloned gene is described. The method is based on controlled use of polymerases. Four populations of DNA molecules are first generated by primer elongation so that they terminate randomly, but always just before a known type of base (before A, C, G or T respectively). Each of the four populations is then mutagenized in a separate misincorporation reaction, where the correct base can now be omitted. The regeneration of wild-type sequences can thus be efficiently avoided. Also, the misincorporating nucleotide concentrations can be optimized to give the three possible single mutations in close to equal ratio. The mutagenesis can be precisely localized within a predetermined target region of any size, and vector sequences remain intact. We have mutagenized the DNA coding for the alpha-fragment of Escherichia coli beta-galactosidase, and identified 176 different base substitution mutations by sequencing. The present method gives mutant yields of 40-60%, when the mutants contain about one amino acid change per protein molecule. All types of base substitution mutations can be generated and deletions are rare. The efficiency of this method permits the use of relatively elaborate screening systems to isolate mutants of either structural genes or regulatory regions.

MeSH Terms
Amino Acid Sequence Base Sequence Cloning, Molecular DNA-Directed DNA Polymerase/genetics Escherichia coli/enzymology Genes, Bacterial Genetic Engineering/methods Molecular Sequence Data Mutation beta-Galactosidase/genetics
Chemicals
DNA-Directed DNA Polymerase beta-Galactosidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Lehtovaara P M
VTT Biotechnical Laboratory, Espoo, Finland.
Koivula A K
Bamford J
Knowles J K
Article Info
Journal
Protein engineering
Abbr.
Protein Eng
ISSN
0269-2139
Published
1988-04-00
Pages
63-8
Language
English
Region
England
NLM ID
8801484
Subset
IM
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