Cloning, sequencing and expression of ribonucleotide reductase R2 from Trypanosoma brucei
Open Access
- 8 September 1997
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 414 (2) , 449-453
- https://doi.org/10.1016/s0014-5793(97)01036-3
Abstract
Ribonucleotide reductase (RR) is an attractive drug target molecule. The gene of the R2 protein of Trypanosoma brucei RR (nrd B) has been cloned. It encodes a protein of 337 residues which shows about 60% identity with other eukaryotic R2 proteins. All residues which bind the iron center, the tyrosyl radical or are supposed to participate in the radical transfer are conserved in the trypanosomal protein sequence. Overexpression of the gene in E. coli resulted in 2–5 mg pure R2 protein from 100 ml bacterial cell culture. Northern blot analysis revealed a transcript of 1.85 kb in bloodstream and procyclic forms of the parasite.Keywords
This publication has 29 references indexed in Scilit:
- The evolution of ribonucleotide reductionTrends in Biochemical Sciences, 1997
- The Three-dimensional Structure of Mammalian Ribonucleotide Reductase Protein R2 Reveals a More-accessible Iron-radical Site thanEscherichia coliR2Journal of Molecular Biology, 1996
- Evidence by Site-Directed Mutagenesis Supports Long-Range Electron Transfer in Mouse Ribonucleotide ReductaseBiochemistry, 1995
- A potent peptidomimetic inhibitor of HSV ribonucleotide reductase with antiviral activity in vivoNature, 1994
- Developmental regulation of Trypanosoma brucei cytochrome c reductase during bloodstream to procyclic differentiationMolecular and Biochemical Parasitology, 1994
- Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interactionBiochemistry, 1992
- The carboxyl terminus heptapeptide of the R2 subunit of mammalian ribonucleotide reductase inhibits enzyme activity and can be used to purify the R1 subunitFEBS Letters, 1990
- Three-dimensional structure of the free radical protein of ribonucleotide reductaseNature, 1990
- The ribonucleotide reductases — A unique group of metalloenzymes essential for cell proliferationPublished by Springer Nature ,1983
- Hydroxyurea: Effect On Growth, Structure, and [3H]Thymidine Uptake of Trypanosoma Brucei Procyclic Culture FormsThe Journal of Protozoology, 1980