ArticleProtein expression and purification2010
Refolding active human DNA polymerase nu from inclusion bodies.
Article in Protein expression and purification, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Analysis of DNA polymerase ν function in meiotic recombination, immunoglobulin class-switching, and DNA damage tolerance.PLoS genetics · 2017Article
- How a homolog of high-fidelity replicases conducts mutagenic DNA synthesis.Nature structural & molecular biology · 2015Article
- Expression, high-pressure refolding, purification, crystallization and preliminary X-ray analysis of a novel single-strand-specific 3'-5' exonuclease PhoExo I from Pyrococcus horikoshii OT3.Acta crystallographica. Section F, Structural biology communications · 2014Article
- A strategy for the expression of recombinant proteins traditionally hard to purify.Analytical biochemistry · 2012Article
- Kinetic analysis of the unique error signature of human DNA polymerase ν.Biochemistry · 2011Article
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Authors and funding
5 authors.
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Abstract
Human DNA polymerase nu (Pol nu) is a conserved family A DNA polymerase of uncertain biological function. Physical and biochemical characterization aimed at understanding Pol nu function is hindered by the fact that, when over-expressed in Escherichia coli, Pol nu is largely insoluble, and the small amount of soluble protein is difficult to purify. Here we describe the use of high hydrostatic pressure to refold Pol nu from inclusion bodies, in soluble and active form. The refolded Pol nu has properties comparable to those of the small amount of Pol nu that was purified from the soluble fraction. The approach described here may be applicable to other DNA polymerases that are expressed as insoluble inclusion bodies in E. coli.
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