adiabatic versus nonadiabatic dressed-state dynamics

We discuss how a recent pump-probe study [Kelkensberg et al., Phys. Rev. Lett. 103, 123005 (2009)] of the dissociative ionization of H2, under the combined effect of a single extreme ultraviolet attosecond pulse and an intense near- infrared pulse, actually represents a transition-state spectroscopy of the strong-field dissociation step, i.e., of the (probe-pulse-)dressed H2+ molecular ion. The way the dissociation dynamics is influenced by the duration of the near-infrared probe pulse, and by the time delay between the two pulses, is discussed in terms of adiabatic versus nonadiabatic preparation and transport of time-parametrized Floquet resonances associated with the dissociating molecular ion. Under a long probe pulse, the field-free vibrational states of the initial wave packet are transported, in a one-to-one manner, onto the Floquet resonances defined by the field intensity of the probe pulse and propagated adiabatically under the pulse. As the probe pulse duration shortens, nonadiabatic transitions between the Floquet resonances become important and manifest themselves in two respects: first, as a vibrational shake-up effect occurring near the peak of the short pulse, and second, through strong interference patterns in the fragment's kinetic energy spectrum, viewed as a function of the time delay between the pump and the probe pulses

Trilinear gauge boson couplings and bilepton production in the SU(3)_C X SU(3)_L X U(1)_N models

The trilinear gauge boson couplings in the SU(3)_C X SU(3)_L X U(1)_N (3 - 3 - 1) models are presented. We find that new $Z_2$ does not interact with the usual (in the standard model) gauge bosons $Z, W^\pm$. Based on these results, production of new heavy gauge bosons at high energy colliders such as e^+ e^- is calculated. We show that the cross sections obtained in the 3 - 3 - 1 model with right-handed neutrinos can be one order bigger than the same in the minimal 3 - 3 - 1 model.Comment: 20 pages, 4 figure, late

Live. Tell. Resist.

This edition of First-Gen Voices features the stories and work of 24 first-generation college students at multiple higher education institutions. The aim is to disseminate a story about us, for us, and consequently, the dominant cultures that have yet to learn from our power

Genome-wide H4 K16 acetylation by SAS-I is deposited independently of transcription and histone exchange

The MYST HAT Sas2 is part of the SAS-I complex that acetylates histone H4 lysine 16 (H4 K16Ac) and blocks the propagation of heterochromatin at the telomeres of Saccharomyces cerevisiae. In this study, we investigated Sas2-mediated H4 K16Ac on a genome-wide scale. Interestingly, H4 K16Ac loss in sas2Δ cells outside of the telomeric regions showed a distinctive pattern in that there was a pronounced decrease of H4 K16Ac within the majority of open reading frames (ORFs), but little change in intergenic regions. Furthermore, regions of low histone H3 exchange and low H3 K56 acetylation showed the most pronounced loss of H4 K16Ac in sas2Δ, indicating that Sas2 deposited this modification on chromatin independently of histone exchange. In agreement with the effect of Sas2 within ORFs, sas2Δ caused resistance to 6-azauracil, indicating a positive effect on transcription elongation in the absence of H4 K16Ac. In summary, our data suggest that Sas2-dependent H4 K16Ac is deposited into chromatin independently of transcription and histone exchange, and that it has an inhibitory effect on the ability of PolII to travel through the body of the gene

Histone H4 Lysine 12 Acetylation Regulates Telomeric Heterochromatin Plasticity in Saccharomyces cerevisiae

Recent studies have established that the highly condensed and transcriptionally silent heterochromatic domains in budding yeast are virtually dynamic structures. The underlying mechanisms for heterochromatin dynamics, however, remain obscure. In this study, we show that histones are dynamically acetylated on H4K12 at telomeric heterochromatin, and this acetylation regulates several of the dynamic telomere properties. Using a de novo heterochromatin formation assay, we surprisingly found that acetylated H4K12 survived the formation of telomeric heterochromatin. Consistently, the histone acetyltransferase complex NuA4 bound to silenced telomeric regions and acetylated H4K12. H4K12 acetylation prevented the over-accumulation of Sir proteins at telomeric heterochromatin and elimination of this acetylation caused defects in multiple telomere-related processes, including transcription, telomere replication, and recombination. Together, these data shed light on a potential histone acetylation mark within telomeric heterochromatin that contributes to telomere plasticity