26 research outputs found
High Magnetic Field NMR Studies of LiVGeO, a quasi 1-D Spin System
We report Li pulsed NMR measurements in polycrystalline and single
crystal samples of the quasi one-dimensional S=1 antiferromagnet
LiVGeO, whose AF transition temperature is K.
The field () and temperature () ranges covered were 9-44.5 T and
1.7-300 K respectively. The measurements included NMR spectra, the spin-lattice
relaxation rate (), and the spin-phase relaxation rate (),
often as a function of the orientation of the field relative to the crystal
axes. The spectra indicate an AF magnetic structure consistent with that
obtained from neutron diffraction measurements, but with the moments aligned
parallel to the c-axis. The spectra also provide the -dependence of the AF
order parameter and show that the transition is either second order or weakly
first order. Both the spectra and the data show that has at
most a small effect on the alignment of the AF moment. There is no spin-flop
transition up to 44.5 T. These features indicate a very large magnetic
anisotropy energy in LiVGeO with orbital degrees of freedom playing an
important role. Below 8 K, varies substantially with the orientation
of in the plane perpendicular to the c-axis, suggesting a small energy
gap for magnetic fluctuations that is very anisotropic.Comment: submitted to Phys. Rev.
An advanced bioinformatics approach for analyzing RNA-seq data reveals sigma H-dependent regulation of competence genes in Listeria monocytogenes
Mutation of a U2 snRNA gene causes global disruption of alternative splicing and neurodegeneration.
Although uridine-rich small nuclear RNAs (U-snRNAs) are essential for pre-mRNA splicing, little is known regarding their function in the regulation of alternative splicing or of the biological consequences of their dysfunction in mammals. Here, we demonstrate that mutation of Rnu2-8, one of the mouse multicopy U2 snRNA genes, causes ataxia and neurodegeneration. Coincident with the observed pathology, the level of mutant U2 RNAs was highest in the cerebellum and increased after granule neuron maturation. Furthermore, neuron loss was strongly dependent on the dosage of mutant and wild-type snRNA genes. Comprehensive transcriptome analysis identified a group of alternative splicing events, including the splicing of small introns, which were disrupted in the mutant cerebellum. Our results suggest that the expression of mammalian U2 snRNA genes, previously presumed to be ubiquitous, is spatially and temporally regulated, and dysfunction of a single U2 snRNA causes neuron degeneration through distortion of pre-mRNA splicing
Loss of Clcc1 Results in ER Stress, Misfolded Protein Accumulation, and Neurodegeneration.
Folding of transmembrane and secretory proteins occurs in the lumen of the endoplasmic reticulum (ER) before transportation to the cell surface and is monitored by the unfolded protein response (UPR) signaling pathway. The accumulation of unfolded proteins in the ER activates the UPR that restores ER homeostasis by regulating gene expression that leads to an increase in the protein-folding capacity of the ER and a decrease in the ER protein-folding load. However, prolonged UPR activity has been associated with cell death in multiple pathological conditions, including neurodegeneration. Here, we report a spontaneous recessive mouse mutation that causes progressive cerebellar granule cell death and peripheral motor axon degeneration. By positional cloning, we identify the mutation in this strain as a retrotransposon insertion in the Clcc1 gene, which encodes a putative chloride channel localized to the ER. Furthermore, we demonstrate that the C3H/HeSnJ inbred strain has late onset cerebellar degeneration due to this mutation. Interestingly, acute knockdown of Clcc1 expression in cultured cells increases sensitivity to ER stress. In agreement, GRP78, the major HSP70 family chaperone in the ER, is upregulated in Clcc1-deficient granule cells in vivo, and ubiquitinated proteins accumulate in these neurons before their degeneration. These data suggest that disruption of chloride homeostasis in the ER disrupts the protein-folding capacity of the ER, leading to eventual neuron death. J Neurosci 2015 Feb 18; 35(7):3001-9