Electric-Field-Induced Energy Tuning of On-Demand Entangled-Photon Emission from Self-Assembled Quantum Dots.

We explore a method to achieve electrical control over the energy of on-demand entangled-photon emission from self-assembled quantum dots (QDs). The device used in our work consists of an electrically tunable diode-like membrane integrated onto a piezoactuator, which is capable of exerting a uniaxial stress on QDs. We theoretically reveal that, through application of the quantum-confined Stark effect to QDs by a vertical electric field, the critical uniaxial stress used to eliminate the fine structure splitting of QDs can be linearly tuned. This feature allows experimental realization of a triggered source of energy-tunable entangled-photon emission. Our demonstration represents an important step toward realization of a solid-state quantum repeater using indistinguishable entangled photons in Bell state measurements.

Localized Surface Plasmons Selectively Coupled to Resonant Light in Tubular Microcavities.

Vertical gold nanogaps are created on microtubular cavities to explore the coupling between resonant light supported by the microcavities and surface plasmons localized at the nanogaps. Selective coupling of optical axial modes and localized surface plasmons critically depends on the exact location of the gold nanogap on the microcavities, which is conveniently achieved by rolling up specially designed thin dielectric films into three-dimensional microtube cavities. The coupling phenomenon is explained by a modified quasipotential model based on perturbation theory. Our work reveals the coupling of surface plasmon resonances localized at the nanoscale to optical resonances confined in microtubular cavities at the microscale, implying a promising strategy for the investigation of light-matter interactions.

Rolled-up TiO2 optical microcavities for telecom and visible photonics.

The fabrication of high-quality-factor polycrystalline TiO2 vertically rolled-up microcavities (VRUMs) by the controlled release of differentially strained TiO2 bilayered nanomembranes, operating at both telecom and visible wavelengths, is reported. Optical characterization of these resonators reveals quality factors as high as 3.8×10³ in the telecom wavelength range (1520-1570 nm) by interfacing a TiO2 VRUMs with a tapered optical fiber. In addition, a splitting in the fundamental modes is experimentally observed due to the broken rotational symmetry in our resonators. This mode splitting indicates coupling between clockwise and counterclockwise traveling whispering gallery modes of the VRUMs. Moreover, we show that our biocompatible rolled-up TiO2 resonators function at several positions along the tube, making them promising candidates for multiplexing and biosensing applications.

Observation of higher order radial modes in atomic layer deposition reinforced rolled-up microtube ring resonators.

We present a detailed investigation of the resonator properties of high-quality rolled-up SiO2 optical microtubes reinforced by atomic layer deposition. The evolution of the resonant modes with increasing film thickness and the transition to a multimode regime, including higher order radial modes, is discussed. Measurements and simulations show that the higher order modes exhibit high optical quality and an increased extension of the evanescent field from the resonator into the surrounding matrix, making them a promising solution for future on-chip sensor applications with increased sensitivity.

High-throughput protoplast transactivation (PTA) system for the analysis of Arabidopsis transcription factor function.

Genomic approaches have generated large Arabidopsis open reading frame (ORF) collections. However, molecular tools are required to characterize this ORFeome functionally. A high-throughput microtiter plate-based protoplast transactivation (PTA) system has been established that can be used in a screening approach to define which transcription factor (TF) regulates a given promoter in planta. Using to this procedure, the transactivation properties of 96 TFs can be analyzed rapidly, making use of promoter:Luciferase (LUC)-reporters and luciferase imaging. Applying GATEWAY® technology, we have established a platform to assay more than 700 Arabidopsis TFs. As a proof-of-principle, the ethylene response factor (ERF) family has been studied to evaluate this system. Importantly, distinct subsets of related ERF factors were found to activate specifically the well described target promoters RD29A and PDF1.2 that are under control of DRE or GCC box cis-elements, respectively. Furthermore, several applications of the PTA system have been demonstrated, such as analysis of transcriptional repressors, salt-inducible gene expression or functional interaction of signaling molecules like kinases and TFs. This novel molecular tool will improve functional studies on transcriptional regulation in plants significantly.

Sharp whispering-gallery modes in rolled-up vertical SiO2 microcavities with quality factors exceeding 5000.

Record high quality (Q) factors of 5400 in vertical microtube ring resonators operated in emission mode are demonstrated. This is achieved by rolling-up a differentially strained SiO2 layer. We also present a theoretical model to investigate the limit of the Q factor. This model especially includes the effect of interlayer voids in the rolled-up geometry, which is found to have a larger effect than scattering due to notches in the spiral shape.

Homo- and heterodimers of tobacco bZIP proteins counteract as positive or negative regulators of transcription during pollen development.

Expression of BZI-1 Delta N, a dominant-negative form of the tobacco (Nicotiana tabacum) basic leucine zipper (bZIP) transcription factor BZI-1 leads to severe defects in pollen development which coincides with reduced transcript abundance of the stamen specific invertase gene NIN88 and decreased extracellular invertase enzymatic activity. This finding suggests a function of BZI-1 in regulating carbohydrate supply of the developing pollen. BZI-1 heterodimerises with the bZIP factors BZI-2, BZI-3 and BZI-4 in vitro and in planta. Whereas BZI-1 exhibits only weak activation properties, BZI-1/BZI-2 heterodimers strongly activate transcription. Consistently, approaches leading to reduced levels of functional BZI-1 or BZI-2 both significantly interfere with pollen development, auxin responsiveness and carbohydrate partitioning. In situ hybridisation studies for BZI-1 and BZI-2 confirmed temporal and spatial overlapping expression patterns in tapetum and pollen supporting functional cooperation of these factors during pollen development. Plants over-expressing BZI-4 produce significantly reduced amounts of intact pollen and are also impaired in NIN88 transcription and enzymatic activity. BZI-4 homodimer efficiently binds to a G-box located in the NIN88 promoter but exhibits almost no transcriptional activation capacity. As BZI-4 does not actively repress transcription, we propose that its homodimer blocks G-box mediated transcription. In summary, these data support a regulatory model in which BZI-4 homodimers and BZI-1/BZI-2 heterodimers perform opposing functions as negative or positive transcriptional regulators during pollen development.

Nuclear accumulation of the ankyrin repeat protein ANK1 enhances the auxin-mediated transcription accomplished by the bZIP transcription factors BZI-1 and BZI-2.

The tobacco (Nicotiana tabacum) basic leucine zipper (bZIP) transcription factor BZI-1 has been implicated in auxin-mediated gene regulation. Yeast two-hybrid analysis has led to the identification of two BZI-1 protein interaction partners: the heterodimerizing bZIP factor BZI-2 and an ankyrin repeat domain protein, ANK1. Analysis in transgenic plants confirms that low levels of functional BZI-1, BZI-2 and ANK1 result in reduced auxin responses. This finding indicates that the three proteins act in the same functional context. The in vivo interaction of ANK1 and BZI-1 has been confirmed by protoplast two-hybrid analysis, as well as by bimolecular fluorescence complementation (BiFC) studies. Whereas YFP-BZI-1 has been found to be localized in the nucleus, YFP-ANK1 resides in the cytosol. Nevertheless, the inhibition of nuclear export with the inhibitor leptomycin B (LMB) and the co-expression with BZI-1, as well as treatment with auxin, results in the accumulation of YFP-ANK1 in the nucleus. Whereas BZI-1 is a weak activator, BZI-1/BZI-2 heterodimers efficiently support transcription. Importantly, conditions that lead to the accumulation of ANK1 in the nucleus, such as the expression of an ANK1 protein fused to a nuclear localization sequence (NLS) or auxin treatment, lead to a significant enhancement of BZI-1/BZI-2-mediated transcription. We therefore propose a mechanism in which the nuclear accumulation of ANK1 enhances BZI-1/BZI-2-mediated transcription in an auxin-dependent manner, presumably facilitated by protein-protein interaction. In summary, this study defines novel components in auxin-dependent signalling and transcriptional control.

The alpha-helical D1 domain of the tobacco bZIP transcription factor BZI-1 interacts with the ankyrin-repeat protein ANK1 and is important for BZI-1 function, both in auxin signaling and pathogen response.

The tobacco (Nicotiana tabacum) bZIP transcription factor BZI-1 is involved in auxin-mediated growth responses and in establishing pathogen defenses. Transgenic plants expressing a dominant-negative BZI-1-DeltaN derivative, which lacks the N-terminal activation domain, showed altered vegetative growth. In particular auxin-induced rooting and formation of tobacco mosaic virus-induced hypersensitive response lesions are affected. BZI-1-related proteins described in various plant species share the conserved domains D1, D2, BD, and D4. To define those BZI-1 domains involved in transcription factor function, BZI-1 deletion derivatives were expressed in transgenic plants. The domains D1 or BD are crucial for BZI-1-DeltaN function in planta. The basic BD domain is mediating DNA binding of BZI-1. Yeast two-hybrid and in vitro binding studies reveal the ankyrin-repeat protein ANK1, which specifically interacts with a part of the BZI-1 protein (amino acids 73-222) encoding the D1 domain. ANK1 does not bind DNA or act as a co-activator of BZI-1-mediated transcription. Moreover, green fluorescence protein localization studies propose that ANK1 is acting mainly inside the cytosol. Transcription analysis reveals that ANK1 is ubiquitously expressed, but after pathogen attack transcription is transiently down-regulated. Along these lines, ANK1 homologous proteins in Arabidopsis thaliana have been reported to function in pathogen defense. We therefore propose that the D1 domain serves as an interaction surface for ANK1, which appears to regulate BZI-1 function in auxin signaling as well as pathogen response.