Journal Articles
Amplifying the Sensitivity of Zinc(II) Responsive MRI Contrast Agents by Altering Water Exchange Rates
Ratio-Controlled Synthesis of CuNi Octahedra and Nanocubes with Enhanced Catalytic Activity
Chemical Characterization of an Alkali-Like Superatom Consisting of a Ta-Encapsulating Si16 Cage
The Metallic State in Neutral Radical Conductors: Dimensionality, Pressure and Multiple Orbital Effects
Caenorhabditis elegans NONO-1: Insights into DBHS protein structure, architecture, and function
Members of the Drosophila behavior/human splicing (DBHS) protein family have been characterized in the vertebrates Homo sapiens and Mus musculus, and the invertebrates Drosophila melanogaster and Chironomus tentans. Collectively, both vertebrate and invertebrate DBHS proteins function throughout gene regulation, largely but not always, within the nucleus. In this study, we report a structural and bioinformatic analysis of the DBHS protein family to guide future studies into DBHS protein function. To explore the structural plasticity of the family, we describe the 2.4 Å crystal structure of Caenorhabditis elegans non-POU domain-containing octamer-binding protein 1 (NONO-1). The structure is dimeric, with a domain arrangement consistent with mammalian DBHS proteins. Comparison with the DBHS structures available from H. sapiens reveals that there is inherent domain flexibility within the homologous DBHS region. Mapping amino acid similarity within the family to the NONO-1 dimer highlights the dimer interface, coiled-coil oligomerization motif, and putative RNA binding surfaces. Surprisingly, the interior surface of RNA recognition motif 2 (RRM2) that faces a large internal void is highly variable, but the external β2–β3 loops of RRM2 show remarkable preservation. Overall, the DBHS region is under strong purifying selection, whereas the sequences N- and C-terminal to the DBHS region are less constrained. The findings described in this study provide a molecular basis for further investigation into the mechanistic function of the DBHS protein family in biology.
Crystal structure of a conserved domain in the intermembrane space region of the plastid division protein ARC6
The chloroplast division machinery is composed of numerous proteins that assemble as a large complex to divide double-membraned chloroplasts through binary fission. A key mediator of division-complex formation is ARC6, a chloroplast inner envelope protein and evolutionary descendant of the cyanobacterial cell division protein Ftn2. ARC6 connects stromal and cytosolic contractile rings across the two membranes through interaction with an outer envelope protein within the intermembrane space (IMS). The ARC6 IMS region bears a structurally uncharacterized domain of unknown function, DUF4101, that is highly conserved among ARC6 and Ftn2 proteins. Here we report the crystal structure of this domain from Arabidopsis thaliana ARC6. The domain forms an α/β barrel open towards the outer envelope membrane but closed towards the inner envelope membrane. These findings provide new clues into how ARC6 and its homologs contribute to chloroplast and cyanobacterial cell division.
The unusual internal motion of the villin headpiece subdomain
The thermostable 36-residue subdomain of the villin headpiece (HP36) is the smallest known cooperatively folding protein. Although the folding and internal dynamics of HP36 and close variants have been extensively studied, there has not been a comprehensive investigation of side-chain motion in this protein. Here, the fast motion of methyl-bearing amino acid side chains is explored over a range of temperatures using site-resolved solution nuclear magnetic resonance deuterium relaxation. The squared generalized order parameters of methyl groups extensively spatially segregate according to motional classes. This has not been observed before in any protein studied using this methodology. The class segregation is preserved from 275 to 305 K. Motions detected in Helix 3 suggest a fast timescale of conformational heterogeneity that has not been previously observed but is consistent with a range of folding and dynamics studies. Finally, a comparison between the order parameters in solution with previous results based on solid-state nuclear magnetic resonance deuterium line shape analysis of HP36 in partially hydrated powders shows a clear disagreement for half of the sites. This result has significant implications for the interpretation of data derived from a variety of approaches that rely on partially hydrated protein samples.
Jin et al. reply
Jin et al. reply
Nature 526, 7575 (2015). doi:10.1038/nature15547
Authors: F.-F. Jin, J. Boucharel & I.-I. Lin
replying to I.-L. Moon, S.-H. Kim & C. Wang Nature526, http://dx.doi.org/10.1038/nature15546 (2015)Observational and modelling studies suggest that subsurface ocean temperature plays a major part in tropical cyclone intensification. In a recent Letter we reported that through
Clustering and percolation in protein loop structures
ToPASeq: an R package for topology-based pathway analysis of microarray and RNA-Seq data
Palladium-Catalyzed Carbonylative Couplings of Vinylogous Enolates: Application to Statin Structures
From Ribbons to Networks: Hierarchical Organization of DNA-Grafted Supramolecular Polymers
Capture of Reactive Monophosphine-Ligated Palladium(0) Intermediates by Mass Spectrometry
Porphyrin Cosensitization for a Photovoltaic Efficiency of 11.5%: A Record for Non-Ruthenium Solar Cells Based on Iodine Electrolyte
Spherical Nanoparticle Supported Lipid Bilayers for the Structural Study of Membrane Geometry-Sensitive Molecules
Metal–Organic Frameworks for Electrocatalytic Reduction of Carbon Dioxide
Correction to “Dynamics of Energy Transfer in a Conjugated Dendrimer Driven by Ultrafast Localization of Excitations”
Success against blindness encourages gene therapy researchers
Success against blindness encourages gene therapy researchers
Nature 526, 7574 (2015). http://www.nature.com/doifinder/10.1038/526487a
Author: Heidi Ledford
Positive news buoys a beleaguered field, but treatment benefits may fade.
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