Theory of phase-locking in generalized hybrid Josephson junction arrays

A recently proposed scheme for the analytical treatment of the dynamics of two-dimensional hybrid Josephson junction arrays is extended to a class of generalized hybrid arrays with ''horizontal'' shunts involving a capacitive as well as an inductive component. This class of arrays is of special interest, because the internal cell coupling has been shown numerically to favor in-phase synchronization for certain parameter values. As a result, we derive limits on the circuit design parameters for realizing this state. In addition, we obtain formulas for the flux-dependent frequency including flux-induced switching processes between the in-phase and anti-phase oscillation regime. The treatment covers unloaded arrays as well as arrays shunted via an external load.Comment: 24 pages, REVTeX, 5 Postscript figures, Subm. to Phys. Rev.

Transcription in the absence of histone H3.3

Di- and trimethylation of histone H3 lysine 4 (H3K4me2 and H3K4me3) are hallmarks of chromatin at active genes. The major fraction of K4-methylated histone H3 is the variant H3 (termed H3.3 in Drosophila), which replaces canonical H3 (H3.2) in transcribed genes. Here, we genetically address the in vivo significance of such K4 methylation by replacing wild-type H3.3 with a mutant form (H3.3K4A) that cannot be methylated. We monitored the transcription that occurs in response to multiple well-described signaling pathways. Surprisingly, the transcriptional outputs of these pathways remain intact in H3.3K4A mutant cells. Even the complete absence of both H3.3 genes does not noticeably affect viability or function of cells: double mutant animals are viable but sterile. Fertility can be rescued by K4-containing versions of H3.3, but not with mutant H3.3 (H3.3K4A) or with canonical H3.2. Together, these data suggest that in Drosophila, presence of H3.3K4me in the chromatin of active genes is dispensable for successful transcription in most cells and only plays an important role in reproductive tissues

Intrinsic mechanism of phase locking in two-dimensional Josephson junction networks in presence of an external magnetic field

We present numerical simulations of the dynamics of two-dimensional Josephson junction arrays to study the mechanism of mutual phase locking. We show that in the presence of an external magnetic field two mechanisms are playing a role in phase locking: feedback through the external load and internal coupling between rows due to microwave currents induced by the field. We have found the parameter values (junction capacitance, cell loop inductance, impedance of the external load) for which the interplay of both these mechanisms leads to the in-phase solution. The case of unshunted arrays is discussed as well.Comment: 13 pages, incl. 6 ps figures, Subm. to Europhysics Letter

Anti-phase locking in a two-dimensional Josephson junction array

We consider theoretically phase locking in a simple two-dimensional Josephson junction array consisting of two loops coupled via a joint line transverse to the bias current. Ring inductances are supposed to be small, and special emphasis is taken on the influence of external flux. Is is shown, that in the stable oscillation regime both cells oscillate with a phase shift equal to $\pi$ (i.e. anti-phase). This result may explain the low radiation output obtained so far in two-dimensional Josephson junction arrays experimentally.Comment: 11 pages, REVTeX, 1 Postscript figure, Subm. to Appl. Phys. Let

Ebola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis

AbstractEbola virus (EBOV) is an enveloped negative-sense RNA virus that causes sporadic outbreaks with high case fatality rates. Ebola viral protein 30 (eVP30) plays a critical role in EBOV transcription initiation at the nucleoprotein (eNP) gene, with additional roles in the replication cycle such as viral assembly. However, the mechanistic basis for how eVP30 functions during the virus replication cycle is currently unclear. Here we define a key interaction between eVP30 and a peptide derived from eNP that is important to facilitate interactions leading to the recognition of the RNA template. We present crystal structures of the eVP30 C-terminus in complex with this eNP peptide. Functional analyses of the eVP30–eNP interface identify residues that are critical for viral RNA synthesis. Altogether, these results support a model where the eVP30–eNP interaction plays a critical role in transcription initiation and provides a novel target for the development of antiviral therapy.</jats:p