125 GeV Higgs as a pseudo-Goldstone boson in supersymmetry with vector-like matters

We propose a possibility of the 125 GeV Higgs being a pseudo-Goldstone boson in supersymmetry with extra vector-like fermions. Higgs mass is obtained from loops of top quark and vector-like fermions from the global symmetry breaking scale f at around TeV. The mu, Bmu/mu \sim f are generated from the dynamics of global symmetry breaking and the Higgs quartic coupling vanishes at f as tan beta \simeq 1. The relation of msoft \sim $4\pi M_Z$ with f \sim mu \sim m_soft \sim TeV is obtained and large mu does not cause a fine tuning for the electroweak symmetry breaking. The Higgs to di-photon rate can be enhanced from the loop of uncolored vector-like matters. The stability problem of Higgs potential with vector-like fermions can be nicely cured by the UV completion with the Goldstone picture.Comment: 28 pages, 8 figure

Imprinting of an evolutionarily conserved antisense transcript gene APeg3

APeg3 is an antisense transcript gene of Peg3, which has been recently identified from rat brain. Careful analyses of EST databases indicated that a homologous transcript also exists in other mammalian species, including mouse, cow and human. 5′-and 3′-RACE experiments have subsequently identified a 900-bp cDNA sequence of APeg3 from mouse brain. Mouse APeg3 is localized in the 3′UTR of Peg3 with an intronless genomic structure. The expression of mouse APeg3 is derived mainly from the paternal allele, indicating the imprinting of this antisense transcript gene in brain. Strand-specific RNA analyses also revealed the expression of both human and cow APEG3 in adult brains. In sum, our study confirms that the mammalian PEG3 locus harbors an antisense transcript gene displaying paternal allele-specific expression, and the evolutionary conservation further suggests potential roles of this transcript gene for the function of this imprinted domain

MacroH2A1 knockdown effects on the Peg3 imprinted domain

<p>Abstract</p> <p>Background</p> <p>MacroH2A1 is a histone variant that is closely associated with the repressed regions of chromosomes. A recent study revealed that this histone variant is highly enriched in the inactive alleles of Imprinting Control Regions (ICRs).</p> <p>Results</p> <p>The current study investigates the potential roles of macroH2A1 in genomic imprinting by lowering the cellular levels of the macroH2A1 protein. RNAi-based macroH2A1 knockdown experiments in Neuro2A cells changed the expression levels of a subset of genes, including <it>Peg3 </it>and <it>Usp29 </it>of the <it>Peg3 </it>domain. The expression of these genes was down-regulated, rather than up-regulated, in response to reduced protein levels of the potential repressor macroH2A1. This down-regulation was not accompanied with changes in the DNA methylation status of the <it>Peg3 </it>domain.</p> <p>Conclusion</p> <p>MacroH2A1 may not function as a transcriptional repressor for this domain, but that macroH2A1 may participate in the heterochromatin formation with functions yet to be discovered.</p

Two evolutionarily conserved sequence elements for Peg3/Usp29 transcription

<p>Abstract</p> <p>Background</p> <p>Two evolutionarily Conserved Sequence Elements, CSE1 and CSE2 (YY1 binding sites), are found within the 3.8-kb CpG island surrounding the bidirectional promoter of two imprinted genes, <it>Peg3 </it>(Paternally expressed gene 3) and <it>Usp29 </it>(Ubiquitin-specific protease 29). This CpG island is a likely ICR (Imprinting Control Region) that controls transcription of the 500-kb genomic region of the <it>Peg3 </it>imprinted domain.</p> <p>Results</p> <p>The current study investigated the functional roles of CSE1 and CSE2 in the transcriptional control of the two genes, <it>Peg3 </it>and <it>Usp29</it>, using cell line-based promoter assays. The mutation of 6 YY1 binding sites (CSE2) reduced the transcriptional activity of the bidirectional promoter in the <it>Peg3 </it>direction in an orientation-dependent manner, suggesting an activator role for CSE2 (YY1 binding sites). However, the activity in the <it>Usp29 </it>direction was not detectable regardless of the presence/absence of YY1 binding sites. In contrast, mutation of CSE1 increased the transcriptional activity of the promoter in both the <it>Peg3 </it>and <it>Usp29 </it>directions, suggesting a potential repressor role for CSE1. The observed repression by CSE1 was also orientation-dependent. Serial mutational analyses further narrowed down two separate 6-bp-long regions within the 42-bp-long CSE1 which are individually responsible for the repression of <it>Peg3 </it>and <it>Usp29</it>.</p> <p>Conclusion</p> <p>CSE2 (YY1 binding sites) functions as an activator for <it>Peg3 </it>transcription, while CSE1 acts as a repressor for the transcription of both <it>Peg3 </it>and <it>Usp29</it>.</p

Structural and Thermal Stabilities of LixCoO2 cathode for LIB studied by a temperature programmed reduction (TPR).

In recent years, research and development of battery technology has primarily been focused on the lithium-ion batteries (LIB) due to the high specific energy density, and therefore are widely utilized as the energy source for portable electronics and electric vehicles. However, the battery safety is an essential issue to overcome, as the battery are required higher power density and larger capacity. Many efforts have been conducted to improve the safety of LIB in the active material processing, as well as the cell battery manufacturing and management technology

HnRNP Q Has a Suppressive Role in the Translation of Mouse Cryptochrome1

Precise regulation of gene expression is especially important for circadian timekeeping which is maintained by the proper oscillation of the mRNA and protein of clock genes and clock-controlled genes. As a main component of the core negative arm feedback loops in the circadian clock, the Cry1 gene contributes to the maintenance of behavioral and molecular rhythmicity. Despite the central role of Cry1, the molecular mechanisms regulating expression levels of Cry1 mRNA and protein are not well defined. In particular, the post-transcriptional regulation of Cry1 mRNA fate decisions is unclear. Here, we demonstrate that hnRNP Q binds to mCry1 mRNA via the 5&apos;UTR. Furthermore, hnRNP Q inhibits the translation of mCry1 mRNA, leading to altered rhythmicity in the mCRY1 protein profile.1145Ysciescopu