A 160Gb/s (4x40) WDM O-band Tx subassembly using a 4-ch array of silicon rings co-packaged with a SiGe BiCMOS IC driver

We present a 400 (8×50) Gb/s-capable RM-based Si-photonic WDM O-band TxRx with 1.17nm channel spacing for high-speed optical interconnects and demonstrate successful 50Gb/s-NRZ TxRx operation achieving a ~4.5dB Tx extinction ratio under 2.15Vpp drive

Dynamics of phosphodiester synthesis by DNA ligase

Ligases are essential actors in DNA replication, recombination, and repair by virtue of their ability to seal breaks in the phosphodiester backbone. Ligation proceeds through a nicked DNA-adenylate intermediate (AppDNA), which must be sealed quickly to avoid creating a potentially toxic lesion. Here, we take advantage of ligase-catalyzed AMP-dependent incision of a single supercoiled DNA molecule to observe the step of phosphodiester synthesis in real time. An exponentially distributed number of supercoils was relaxed per successful incision-resealing event, from which we deduce the torque-dependent ligation probability per DNA swivel. Premature dissociation of ligase from nicked DNA-adenylate accounted for ≈10% of the observed events. The ability of ligase to form a C-shaped protein clamp around DNA is a key determinant of ligation probability per turn and the stability of the ligase-AppDNA intermediate. The estimated rate of phosphodiester synthesis by DNA ligase (400 s−1) is similar to the high rates of phosphodiester synthesis by replicative DNA polymerases

The associative nature of adenylyl transfer catalyzed by T4 DNA ligase

DNA ligase seals nicks in dsDNA using chemical energy of the phosphoanhydride bond in ATP or NAD+ and assistance of a divalent metal cofactor Mg2+. Molecular details of ligase catalysis are essential for understanding the mechanism of metal-promoted phosphoryl transfer reactions in the living cell responsible for a wide range of processes, e.g., DNA replication and transcription, signaling and differentiation, energy coupling and metabolism. Here we report a single-turnover 31P solid-state NMR study of adenylyl transfer catalyzed by DNA ligase from bacteriophage T4. Formation of a high-energy covalent ligase–nucleotide complex is triggered in situ by the photo release of caged Mg2+, and sequentially formed intermediates are monitored by NMR. Analyses of reaction kinetics and chemical-shift changes indicate that the pentacoordinated phosphorane intermediate builds up to 35% of the total reacting species after 4–5 h of reaction. This is direct experimental evidence of the associative nature of adenylyl transfer catalyzed by DNA ligase. NMR spectroscopy in rotating solids is introduced as an analytical tool for recording molecular movies of reaction processes. Presented work pioneers a promising direction in structural studies of biochemical transformations