244 research outputs found
Neoclassical transport of tungsten ion bundles in total-f neoclassical gyrokinetic simulations of a whole-volume JET-like plasma
Neoclassical gyrokinetic simulations including tungsten impurities are
carried out using multiple gyrokinetic bundles to model the many charge states
of tungsten ions present in the whole-volume of a model H-mode plasma in JET
geometry. A gyrokinetic bundle regroups tungsten ions of similar charge
together in order to decrease the computational cost. The initial radial shape
of the bundles and their individual charges are deduced from a coronal
approximation and from quasi-neutrality of the plasma. Low-Z tungsten ions move
radially inward from SOL into the core region, whereas high-Z tungsten ions
move radially outwardly from the core and inwardly from the separatrix. These
fluxes lead to an accumulation of tungsten in the pedestal top of our test
case. This organization of the fluxes cannot be captured by a single
tungsten-ion simulation. Large up/down poloidal asymmetries of tungsten form in
the pedestal and strongly influence the direction of these neoclassical fluxes.
Future implementation of atomic interactions between bundles is discussed.Comment: 11 pages, 11 figure
Potential of a plasma bound between two biased walls
An analytical study is presented for an one-dimensional, steady-state plasma bound between two perfectly absorbing walls that are biased with respect to each other. Starting from a description of the plasma sheaths formed at both walls, an expression relating the bulk plasma potential to the wall currents is derived, showing that the plasma potential undergoes an abrupt transition when currents cross a critical value. This result is confirmed by numerical simulations performed with a particle-in-cell code. [http://dx.doi.org/10.1063/1.4745863
ORB5: a global electromagnetic gyrokinetic code using the PIC approach in toroidal geometry
This paper presents the current state of the global gyrokinetic code ORB5 as
an update of the previous reference [Jolliet et al., Comp. Phys. Commun. 177
409 (2007)]. The ORB5 code solves the electromagnetic Vlasov-Maxwell system of
equations using a PIC scheme and also includes collisions and strong flows. The
code assumes multiple gyrokinetic ion species at all wavelengths for the
polarization density and drift-kinetic electrons. Variants of the physical
model can be selected for electrons such as assuming an adiabatic response or a
``hybrid'' model in which passing electrons are assumed adiabatic and trapped
electrons are drift-kinetic. A Fourier filter as well as various control
variates and noise reduction techniques enable simulations with good
signal-to-noise ratios at a limited numerical cost. They are completed with
different momentum and zonal flow-conserving heat sources allowing for
temperature-gradient and flux-driven simulations. The code, which runs on both
CPUs and GPUs, is well benchmarked against other similar codes and analytical
predictions, and shows good scalability up to thousands of nodes
Concentrating pre-mRNA processing factors in the histone locus body facilitates efficient histone mRNA biogenesis
The histone locus body (HLB) assembles at replication-dependent histone genes and concentrates factors required for histone messenger RNA (mRNA) biosynthesis. FLASH (Flice-associated huge protein) and U7 small nuclear RNP (snRNP) are HLB components that participate in 3′ processing of the nonpolyadenylated histone mRNAs by recruiting the endonuclease CPSF-73 to histone pre-mRNA. Using transgenes to complement a FLASH mutant, we show that distinct domains of FLASH involved in U7 snRNP binding, histone pre-mRNA cleavage, and HLB localization are all required for proper FLASH function in vivo. By genetically manipulating HLB composition using mutations in FLASH, mutations in the HLB assembly factor Mxc, or depletion of the variant histone H2aV, we find that failure to concentrate FLASH and/or U7 snRNP in the HLB impairs histone pre-mRNA processing. This failure results in accumulation of small amounts of polyadenylated histone mRNA and nascent read-through transcripts at the histone locus. Thus, the HLB concentrates FLASH and U7 snRNP, promoting efficient histone mRNA biosynthesis and coupling 3′ end processing with transcription termination
A Conserved Interaction That Is Essential for the Biogenesis of Histone Locus Bodies
Nuclear protein, ataxia-telangiectasia locus (NPAT) and FLICE-associated huge protein (FLASH) are two major components of discrete nuclear structures called histone locus bodies (HLBs). NPAT is a key co-activator of histone gene transcription, whereas FLASH through its N-terminal region functions in 3′ end processing of histone primary transcripts. The C-terminal region of FLASH contains a highly conserved domain that is also present at the end of Yin Yang 1-associated protein-related protein (YARP) and its Drosophila homologue, Mute, previously shown to localize to HLBs in Drosophila cells. Here, we show that the C-terminal domain of human FLASH and YARP interacts with the C-terminal region of NPAT and that this interaction is essential and sufficient to drive FLASH and YARP to HLBs in HeLa cells. Strikingly, only the last 16 amino acids of NPAT are sufficient for the interaction. We also show that the C-terminal domain of Mute interacts with a short region at the end of the Drosophila NPAT orthologue, multi sex combs (Mxc). Altogether, our data indicate that the conserved C-terminal domain shared by FLASH, YARP, and Mute recognizes the C-terminal sequence of NPAT orthologues, thus acting as a signal targeting proteins to HLBs. Finally, we demonstrate that the C-terminal domain of human FLASH can be directly joined with its N-terminal region through alternative splicing. The resulting 190-amino acid MiniFLASH, despite lacking 90% of full-length FLASH, contains all regions necessary for 3′ end processing of histone pre-mRNA in vitro and accumulates in HLBs
A Complex Containing the CPSF73 Endonuclease and Other Polyadenylation Factors Associates with U7 snRNP and Is Recruited to Histone Pre-mRNA for 3'-End Processing
Animal replication-dependent histone pre-mRNAs are processed at the 3′ end by endonucleolytic cleavage that is not followed by polyadenylation. The cleavage reaction is catalyzed by CPSF73 and depends on the U7 snRNP and its integral component, Lsm11. A critical role is also played by the 220-kDa protein FLASH, which interacts with Lsm11. Here we demonstrate that the N-terminal regions of these two proteins form a platform that tightly interacts with a unique combination of polyadenylation factors: symplekin, CstF64, and all CPSF subunits, including the endonuclease CPSF73. The interaction is inhibited by alterations in each component of the FLASH/Lsm11 complex, including point mutations in FLASH that are detrimental for processing. The same polyadenylation factors are associated with the endogenous U7 snRNP and are recruited in a U7-dependent manner to histone pre-mRNA. Collectively, our studies identify the molecular mechanism that recruits the CPSF73 endonuclease to histone pre-mRNAs, reveal an unexpected complexity of the U7 snRNP, and suggest that in animal cells polyadenylation factors assemble into two alternative complexes—one specifically crafted to generate polyadenylated mRNAs and the other to generate nonpolyadenylated histone mRNAs that end with the stem-loop
U7 snRNA mutations in Drosophila block histone pre-mRNA processing and disrupt oogenesis
Metazoan replication-dependent histone mRNAs are not polyadenylated, and instead terminate in a conserved stem–loop structure generated by an endonucleolytic cleavage involving the U7 snRNP, which interacts with histone pre-mRNAs through base-pairing between U7 snRNA and a purine-rich sequence in the pre-mRNA located downstream of the cleavage site. Here we generate null mutations of the single Drosophila U7 gene and demonstrate that U7 snRNA is required in vivo for processing all replication-associated histone pre-mRNAs. Mutation of U7 results in the production of poly A+ histone mRNA in both proliferating and endocycling cells because of read-through to cryptic polyadenylation sites found downstream of each Drosophila histone gene. A similar molecular phenotype also results from mutation of Slbp, which encodes the protein that binds the histone mRNA 3′ stem–loop. U7 null mutants develop into sterile males and females, and these females display defects during oogenesis similar to germ line clones of Slbp null cells. In contrast to U7 mutants, Slbp null mutations cause lethality. This may reflect a later onset of the histone pre-mRNA processing defect in U7 mutants compared to Slbp mutants, due to maternal stores of U7 snRNA. A double mutant combination of a viable, hypomorphic Slbp allele and a viable U7 null allele is lethal, and these double mutants express polyadenylated histone mRNAs earlier in development than either single mutant. These data suggest that SLBP and U7 snRNP cooperate in the production of histone mRNA in vivo, and that disruption of histone pre-mRNA processing is detrimental to development
- …