VEGa : a high performance vehicular Ethernet gateway on hybrid FPGA

Modern vehicles employ a large amount of distributed computation and require the underlying communication scheme to provide high bandwidth and low latency. Existing communication protocols like Controller Area Network (CAN) and FlexRay do not provide the required bandwidth, paving the way for adoption of Ethernet as the next generation network backbone for in-vehicle systems. Ethernet would co-exist with safety-critical communication on legacy networks, providing a scalable platform for evolving vehicular systems. This requires a high-performance network gateway that can simultaneously handle high bandwidth, low latency, and isolation; features that are not achievable with traditional processor based gateway implementations. We present VEGa, a configurable vehicular Ethernet gateway architecture utilising a hybrid FPGA to closely couple software control on a processor with dedicated switching circuit on the reconfigurable fabric. The fabric implements isolated interface ports and an accelerated routing mechanism, which can be controlled and monitored from software. Further, reconfigurability enables the switching behaviour to be altered at run-time under software control, while the configurable architecture allows easy adaptation to different vehicular architectures using high-level parameter settings. We demonstrate the architecture on the Xilinx Zynq platform and evaluate the bandwidth, latency, and isolation using extensive tests in hardware

Search Space Reduction for E/E-Architecture Partitioning

Abstract. As the design of electrical/electronic (E/E)-architectures is becoming more complex, multi-objective optimization algorithms such as evolutionary algorithms (EAs) have been proposed for generating resource optimized architectures. In this paper we extend existing approaches by excluding infeasible solutions from the search space and thereby enhance the quality and runtime behavior of the optimization

Phosphorylation of the FACT histone chaperone subunit SPT16 affects chromatin at RNA polymerase II transcriptional start sites in Arabidopsis

The heterodimeric histone chaperone FACT, consisting of SSRP1 and SPT16, contributes to dynamic nucleosome rearrangements during various DNA-dependent processes including transcription. In search of post-translational modifications that may regulate the activity of FACT, SSRP1 and SPT16 were isolated from Arabidopsis cells and analysed by mass spectrometry. Four acetylated lysine residues could be mapped within the basic C-terminal region of SSRP1, while three phosphorylated serine/threonine residues were identified in the acidic C-terminal region of SPT16. Mutational analysis of the SSRP1 acetylation sites revealed only mild effects. However, phosphorylation of SPT16 that is catalysed by protein kinase CK2, modulates histone interactions. A non-phosphorylatable version of SPT16 displayed reduced histone binding and proved inactive in complementing the growth and developmental phenotypes of spt16 mutant plants. In plants expressing the non-phosphorylatable SPT16 version we detected at a subset of genes enrichment of histone H3 directly upstream of RNA polymerase II transcriptional start sites (TSSs) in a region that usually is nucleosome-depleted. This suggests that some genes require phosphorylation of the SPT16 acidic region for establishing the correct nucleosome occupancy at the TSS of active genes

Inducible DNA-loop formation blocks transcriptional activation by an SV40 enhancer

It is well established that gene expression in eukaryotes is controlled by sequence-dependent binding of trans-acting proteins to regulatory elements like promoters, enhancers or silencers. A less well understood level of gene regulation is governed by the various structural and functional states of chromatin, which have been ascribed to changes in covalent modification of core histone proteins. And, much on how topological domains in the genome take part in establishing and maintaining distinct gene expression patterns is still unknown. Here we present a set of regulatory proteins that allow to reversibly alter the DNA structure in vivo and in vitro by adding low molecular weight effectors that control their oligomerization and DNA binding. Using this approach, we completely regulate the activity of an SV40 enhancer in HeLa cells by reversible loop formation to topologically separate it from the promoter. This result establishes a new mechanism for DNA-structure-dependent gene regulation in vivo and provides evidence supporting the structural model of insulator function