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Characterization of a temperature-sensitive DNA ligase from Escherichia coli
DNA ligases are essential enzymes in cells due to their ability to join DNA strand breaks formed during DNA replication. Several temperature-sensitive mutant strains of Escherichia coli, including strain GR501, have been described which can be complemented by functional DNA ligases. Here, it is shown that the ligA251 mutation in E. coli GR501 strain is a cytosine to thymine transition at base 43, which results in a substitution of leucine by phenylalanine at residue 15. The protein product ofdoi:10.1099/mic.0.27287-0 pmid:15583169 fatcat:jhlgwqobhzazhnmaczltemh5bq