Mikael Crona

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Ribonucleotide reductase (RNR) is the only source for de novo production of the four deoxyribonucleoside triphosphate (dNTP) building blocks needed for DNA synthesis and repair. It is crucial that these dNTP pools are carefully balanced, since mutation rates increase when dNTP levels are either unbalanced or elevated. RNR is the major player in this(More)
Ribonucleotide reductase (RNR) is a key enzyme for the synthesis of the four DNA building blocks. Class Ia RNRs contain two subunits, denoted R1 (alpha) and R2 (beta). These enzymes are regulated via two nucleotide-binding allosteric sites on the R1 subunit, termed the specificity and overall activity sites. The specificity site binds ATP, dATP, dTTP, or(More)
Ribonucleotide reductase (RNR) synthesizes deoxyribonucleotides for DNA replication and repair and is controlled by sophisticated allosteric regulation involving differential affinity of nucleotides for regulatory sites. We have developed a robust and sensitive method for coupling biotinylated RNRs to surface plasmon resonance streptavidin biosensor chips(More)
In the present study, we introduce a novel method for in vivo imaging of the biodistribution of single wall carbon nanotubes (SWNTs) labeled with recombinant thermo-stable Luciola cruciata luciferase (LcL). In addition, we highlight a new application for green fluorescent proteins in which they are utilized as imaging moieties for SWNTs. Carbon nanotubes(More)
Ribonucleotide reductases (RNRs) catalyze the only pathway for de novo synthesis of deoxyribonucleotides needed for DNA replication and repair. The vast majority of eukaryotes encodes only a class I RNR, but interestingly some eukaryotes, including the social amoeba Dictyostelium discoideum, encode both a class I and a class II RNR. The amino acid sequence(More)
Ribonucleotide Reductase (RNR) is the sole enzyme that catalyzes the reduction of ribonucleotides into deoxyribonucleotides. Even though RNR is a recognized target for antiproliferative molecules, and the main target of the approved drug hydroxyurea, few new leads targeted to this enzyme have been developed. We have evaluated a recently identified set of(More)
15 Ribonucleotide reductases (RNRs) are key enzymes in DNA synthesis and repair, with 16 sophisticated allosteric mechanisms controlling both substrate specificity and overall activity. 17 In RNRs, the activity master-switch, the ATP-cone, has been found exclusively in the 18 catalytic subunit. In two class I RNR subclasses whose catalytic subunit lacks the(More)
Ribonucleotide reductase (RNR) catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, which are used as building blocks for DNA replication and repair. This process is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone(More)
15 Ribonucleotide reductases (RNRs) are key enzymes in DNA synthesis and repair, with 16 sophisticated allosteric mechanisms controlling both substrate specificity and overall activity. 17 In RNRs, the activity master-switch, the ATP-cone, has been found exclusively in the 18 catalytic subunit. In two class I RNR subclasses whose catalytic subunit lacks the(More)
The opportunistic pathogen Pseudomonas aeruginosa can grow under both aerobic and anaerobic conditions. Its flexibility with respect to oxygen load is reflected by the fact that its genome encodes all three existing classes of ribonucleotides reductase (RNR): the oxygen-dependent class I RNR, the oxygen-indifferent class II RNR, and the oxygen-sensitive(More)