Purification and properties of Aquifex aeolicus DNA polymerase expressed in Escherichia coli.

Abstract:

:The gene encoding Aquifex aeolicus (Aae) DNA polymerase was expressed under the control of the trp promoter on a high-copy plasmid, pTRPNS, in Escherichia coli. The expressed enzyme was purified 11-fold with a 13.8% yield and a specific activity of 2268.3 U mg(-1). The optimum pH of the enzyme was 6.8-7.2. The optimal concentrations of KCl and Mg(2+) were 20-30 mM and 4-5 mM, respectively. Aae DNA polymerase contained a double-strand-dependent 3'-->5' proofreading exonuclease activity but lacked any detectable 5'-->3' exonuclease activity.

journal_name

FEMS Microbiol Lett

authors

Chang JR,Choi JJ,Kim HK,Kwon ST

doi

10.1111/j.1574-6968.2001.tb10735.x

keywords:

subject

Has Abstract

pub_date

2001-07-10 00:00:00

pages

73-7

issue

1

eissn

0378-1097

issn

1574-6968

pii

S0378-1097(01)00248-8

journal_volume

201

pub_type

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