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Bleomycins: towards better therapeutics
Progress in understanding the mechanisms involved in the therapeutic efficacy of the bleomycins and the unwanted toxicity and elucidation of the biosynthetic pathway of theBleomycin sets the stage for developing a more potent, less toxic therapeutic agent. Expand
Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase.
This work proposes that Rnr2-Rnr4 nuclear localization is achieved by a dynamic combination of Wtm1-mediated nuclear retention to limit export and regulated nuclear import through Dif1, which is both cell-cycle and DNA-damage regulated. Expand
Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster.
The study uncovers an important role of monothiol glutaredoxins in cellular iron metabolism, with a surprising connection to cellular redox and sulfur metabolisms. Expand
Phage auxiliary metabolic genes and the redirection of cyanobacterial host carbon metabolism.
It is proposed that phage-augmented NADPH production fuels deoxynucleotide biosynthesis for phage replication, and that the selection pressures molding phage genomes involve fitness advantages conferred through mobilization of host energy stores. Expand
Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: evidence for a required posttranslational modification for catalytic activity.
Results suggest PHA synthase is posttranslationally modified by phosphopantetheine, and this model is based on the well-characterized enzymes involved in fatty acid biosynthesis. Expand
The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production.
Transfer of the R. eutropha phaR, phaP, and PHA biosynthesis (phaCAB) genes into a heterologous system was sufficient to reconstitute thePhaR/PhaP regulatory system, implying that PhaR both regulates PhaP accumulation and responds to PHA directly. Expand
Protein Radicals in Enzyme Catalysis.
Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways
The results suggest a mechanism by which DNA damage checkpoint modulates RNR activity through the temporal and spatial regulation of its subunits. Expand
Enhanced subunit interactions with gemcitabine-5′-diphosphate inhibit ribonucleotide reductases
Isolation of these complexes establishes that the weak interactions of the subunits in the absence of nucleotides are substantially increased in the presence of F2CDP and ATP, and the proposed asymmetry between the interactions of αnβn provide an explanation for complete inactivation of RNR with substoichiometric amounts of F1CDP. Expand
The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer
Surprisingly, the dimer interface responsible for effector binding in class I RNR is preserved through a single 130-residue insertion in the class II structure, which makes L. leichmannii RNR a paradigm for the simplest structural entity capable of ribonucleotide reduction, a reaction linking the RNA and DNA worlds. Expand