PMID:776979: Difference between revisions

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<span style = 'font-size: large'> '''Uyemura, D, Eichler, DC and Lehman, IR'''  (1976) Biochemical characterization of mutant forms of DNA polymerase I from Escherichia coli. II. The polAex1 mutation.''J. Biol. Chem.'' '''251''':4085-9</span>
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|{{TableHeadingColor}} |'''Abstract''' || <protect>DNA polymerase I has been purified to homogeneity from an Escherichia coli K12 strain bearing the temperature-sensitive conditionally lethal mutation, polAex1. The purified enzyme shows no defect in its polymerase or 3' leads to 5'-exonuclease activities; however, its 5' leads to 3'-exonuclease activity is abnormally low at both 30 degrees and 43 degrees. Although the mutant enzyme is able to catalyze the coordinated 5' leads to 3' polymerization and 5' leads to 3' exonucleolytic hydrolysis of nucleotides at a nick in duplex DNA ("nick translation") at a measurable rate at 30 degrees, this reaction is undetectable at 43 degrees. This defect is very likely responsible for the retarded joining of nascent DNA fragments and the consequent loss of viability that occur in the mutant at this temperature.</protect>
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'''No author listed''' (1976) Biochemical characterization of mutant forms of DNA polymerase I from Escherichia coli. II. The polAex1 mutation. ''J. Biol. Chem.'' '''251''':4085-9
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=776979 PubMed]<br/>
!align=left  |Abstract
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DNA polymerase I has been purified to homogeneity from an Escherichia coli K12 strain bearing the temperature-sensitive conditionally lethal mutation, polAex1. The purified enzyme shows no defect in its polymerase or 3' leads to 5'-exonuclease activities; however, its 5' leads to 3'-exonuclease activity is abnormally low at both 30 degrees and 43 degrees. Although the mutant enzyme is able to catalyze the coordinated 5' leads to 3' polymerization and 5' leads to 3' exonucleolytic hydrolysis of nucleotides at a nick in duplex DNA ("nick translation") at a measurable rate at 30 degrees, this reaction is undetectable at 43 degrees. This defect is very likely responsible for the retarded joining of nascent DNA fragments and the consequent loss of viability that occur in the mutant at this temperature.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=776979 PubMed]
 
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DNA Nucleotidyltransferases/metabolism; Escherichia coli/metabolism; Exonucleases/metabolism; Genetic Variation; Kinetics; Mutation; Temperature
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 19:39, 1 September 2013

Citation

No author listed (1976) Biochemical characterization of mutant forms of DNA polymerase I from Escherichia coli. II. The polAex1 mutation. J. Biol. Chem. 251:4085-9

Abstract

DNA polymerase I has been purified to homogeneity from an Escherichia coli K12 strain bearing the temperature-sensitive conditionally lethal mutation, polAex1. The purified enzyme shows no defect in its polymerase or 3' leads to 5'-exonuclease activities; however, its 5' leads to 3'-exonuclease activity is abnormally low at both 30 degrees and 43 degrees. Although the mutant enzyme is able to catalyze the coordinated 5' leads to 3' polymerization and 5' leads to 3' exonucleolytic hydrolysis of nucleotides at a nick in duplex DNA ("nick translation") at a measurable rate at 30 degrees, this reaction is undetectable at 43 degrees. This defect is very likely responsible for the retarded joining of nascent DNA fragments and the consequent loss of viability that occur in the mutant at this temperature.

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Keywords

DNA Nucleotidyltransferases/metabolism; Escherichia coli/metabolism; Exonucleases/metabolism; Genetic Variation; Kinetics; Mutation; Temperature

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