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Iron-sulfur cluster assembly in the eukaryotic cytosol. Netz et al. (p 278) have identified the Cfd1-Nbp35 complex as a scaffold protein for iron-sulfur cluster assembly in the yeast cytosol. The Cfd1-Nbp35 complex can bind up to three [4Fe-4S] clusters and transfer them, both in vitro and in vivo, to target [Fe-S] apoproteins (see also News & Views by Broderick, p 243). Images of [2Fe-2S] and [4Fe- 4S] clusters are shown. The [2Fe-2S] image is from the [2Fe-2S] ferredoxin from Spirulina platensis (PDB ID 4FXC) and the [4Fe-4S] image is from Azotobacter vinelandii ferredoxin (PDB ID 1FDA); both images were prepared using PyMOL. Cover art by Erin Boyle, based on images provided by David Mulder, John Peters and Joan Broderick.
Two proteins that together serve as a scaffold for iron-sulfur cluster assembly in the yeast cytosol have been identified, providing the first mechanistic insight into cytosolic cluster assembly.
Quantitative detection of H2O2, which is increasingly recognized as an intracellular messenger, remains a challenge for cell biologists. The development of molecular probes that fluoresce upon H2O2-mediated removal of a boronate-based protecting group, rather than upon nonspecific oxidation, demonstrates that this challenge is not insurmountable.
A chemical-genetic study indicates that modulation of neurotransmitter signaling affects the self-renewal capacity of neural stem cells in culture. Although the mechanisms of action are not resolved, the research points to a potential therapeutic target class for treatment of brain tumors.
Simultaneous measurement of multiple analytes in high-throughput assays requires the design of integrated sensory elements. The latest development in this field is an engineering masterpiece based on microfluidics, photolithography and polymer science.
Lysine methylation has been implicated in gene transcription and epigenetic control. Chemical modification of cysteine residues results in a highly similar structural and functional analog of methylated lysine and provides a means to study this important modification in nucleosomes.