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T7 DNA polymerase is not a zinc-metalloenzyme and the polymerase and exonuclease activities are inhibited by zinc ions.

Abstract：

:Phage T7 DNA polymerase purified to homogeneity by an antithioredoxin immunoadsorbent technique was resolved into its active subunits the gene 5 protein and Escherichia coli thioredoxin by a novel technique involving chromatography on Sephadex G-50 at pH 11.5. Analysis of the metal content of the holoenzyme by atomic absorption spectroscopy showed that it did not contain stoichiometric amounts of zinc. Determination of polymerase and exonuclease activities of the holoenzyme and the gene 5 protein in assay mixtures containing enzyme concentrations in excess of the Zn2+ concentration showed full activity. Addition of Zn2+ resulted in no stimulation and the activities were completely inhibited by 0.1 mM Zn2+. These results demonstrate that the essential T7 DNA polymerase is not a zinc-metalloenzyme and suggest that DNA polymerases show no functional requirement for Zn2+.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Slaby I,Lind B,Holmgren A

doi

10.1016/0006-291x(84)91248-8

subject

Has Abstract

pub_date

1984-08-16 00:00:00

pages

1410-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(84)91248-8

journal_volume

122

pub_type

杂志文章

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