PMID: 8947477Nov 15, 1996Paper

Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacity

The Biochemical Journal
N LamarcheY Langelier

Abstract

The R2 subunit of ribonucleotide reductase from herpes simplex virus type 2 was overproduced with prokaryotic and eukaryotic expression systems. The recombinant R2 purified by a two-step procedure exhibited a 3-fold higher activity when produced in eukaryotic cells. Precise quantification of the R2 concentration at each step of the purification indicated that the activity was not altered during the purification procedure. Moreover, we have observed that the level of R2 expression, in eukaryotic cells as well as in prokaryotic cells, did not influence R2 activity. Extensive characterization of the recombinant R2 purified from eukaryotic and prokaryotic expression systems has shown that both types of pure R2 preparations were similar in their 76 kDa dimer contents (more than 95%) and in their ability to bind the R1 subunit. However, we have found that the higher activity of R2 produced in eukaryotic cells is more probably related to a higher capability of binding the iron cofactor as well as a 3-fold greater ability to generate the tyrosyl free radical.

Citations

Jan 20, 2010·Cell Biochemistry and Function·Luisa GenneroAgostino Pugliese
Nov 25, 2016·Environmental Research·Filomena FioritoGiuseppe Iovane
Jan 30, 2004·Nature·Edith GouinPascale Cossart
Nov 9, 2007·Journal of Cellular Biochemistry·Carmen MaffettoneAlfredo Colonna
Sep 25, 2009·The American Journal of Clinical Nutrition·Heather A Eicher-MillerCarol J Boushey
Apr 28, 2021·Research in Veterinary Science·Filomena FioritoLuisa De Martino

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