Compact Wideband Coplanar Stripline-to-Microstrip Line Transition Using a Bended Structure on a Two-Layered Substrate

A design of a compact coplanar strip (CPS)-to-microstrip line (MSL) transition using a bended structure on a two-layered substrate is presented. The proposed transition consists of a CPS taper and a bended CPS-to-MSL transition on a two-layered substrate. The CPS taper is formed on the lower substrate with low permittivity (εr = 3.38), and the bended CPS-to-MSL transition is formed on the upper substrate with high permittivity (εr= 10.2). The proposed transition is designed with analytical formulas obtained by applying EM-based conformal mapping without parametric tuning trials. The conductor shape of the bended CPS-to-MSL transition is adjusted to form an optimal Klopfenstein impedance taper. The proposed CPS-to-MSL transition optimally connects between a high impedance CPS line (~160 Ω) and a 50 Ω MSL, which typically results in a long transition length for ultra-wideband performance. The implemented transition bended in a sinusoid shape on the two-layered substrate provides good performance from 2 GHz to 17 GHz with the maximum 2 dB insertion loss per transition, and the horizontal length of the bended transition is reduced to 42.9% of the straight transition length. This bended transition is developed for use in mm-wave balanced antenna/detector feeds but can be applied to a variety of wideband balanced circuit modules, where compact circuit size is critical.

Comprehensive structure-function characterization of DNMT3B and DNMT3A reveals distinctive de novo DNA methylation mechanisms

Mammalian DNA methylation patterns are established by two de novo DNA methyltransferases DNMT3A and DNMT3B, which exhibit both redundant and distinctive methylation activities. However, the related molecular basis remains undetermined. Through comprehensive structural, enzymology and cellular characterization of DNMT3A and DNMT3B, we here report a multi-layered substrate-recognition mechanism underpinning their divergent genomic methylation activities. A hydrogen bond in the catalytic loop of DNMT3B causes a lower CpG specificity than DNMT3A, while the interplay of target recognition domain and homodimeric interface fine-tunes the distinct target selection between the two enzymes, with Lysine 777 of DNMT3B acting as a unique sensor of the +1 flanking base. The divergent substrate preference between DNMT3A and DNMT3B provides an explanation for site-specific epigenomic alterations seen in ICF syndrome with DNMT3B mutations. Together, this study reveals crucial and distinctive substrate-readout mechanisms of the two DNMT3 enzymes, implicative of their differential roles during development and pathogenesis.