PMID: 2115439Jul 5, 1990Paper

Purification and characterization of a DNA polymerase from the archaebacterium Thermoplasma acidophilum

European Journal of Biochemistry
A HamalC Elie

Abstract

A thermophilic DNA polymerase has been purified to near homogeneity from the archaebacterium Thermoplasma acidophilum. Analysis of the purified enzyme by sodium dodecyl sulfate gel electrophoresis revealed a single polypeptide of 88 kDa which co-sediments with the DNA polymerase activity on sucrose gradients. Combination of sedimentation and gel filtration analyses indicates that this DNA polymerase is an 88-kDa monomeric enzyme in its native form. The DNA polymerase is resistant to aphidicolin, slightly sensitive to 2',3'-dideoxyribosylthymine triphosphate and inhibited by N-ethylmaleimide when preincubation with this reagent is performed at 65 degrees C. We find that a 3'----5' exonuclease activity is associated with the purified DNA polymerase; the two activities of the enzyme are optimal at 65 degrees C but the exonuclease activity is active in a broader range of lower temperatures and is more thermostable than the DNA polymerase activity.

References

Jun 1, 1987·Microbiological Reviews·C R Woese
May 2, 1988·European Journal of Biochemistry·W ZilligH P Klenk
Aug 1, 1984·Journal of Bacteriology·P ForterreM Kohiyama

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Citations

Jan 1, 1995·World Journal of Microbiology & Biotechnology·M CiaramellaM Rossi
Mar 7, 2006·Applied and Environmental Microbiology·Hélène MoussardChristian Jeanthon
Nov 1, 2005·Current Opinion in Microbiology·Ksenia Egorova, Garabed Antranikian
Nov 1, 1990·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·J E Syväoja
Jul 1, 1992·Journal of Bacteriology·E SellmannP Westermann
Apr 1, 1997·Journal of Bacteriology·D R EdgellW F Doolittle

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