On-chip photonic microsystem for optical signal processing based on silicon and silicon nitride platforms

The explosive growth of data centers, cloud computing and various smart devices is limited by the current state of microelectronics, both in terms of speed and heat generation. Benefiting from the large bandwidth, promising low power consumption and passive calculation capability, experts believe that the integrated photonics-based signal processing and transmission technologies can break the bottleneck of microelectronics technology. In recent years, integrated photonics has become increasingly reliable and access to the advanced fabrication process has been offered by various foundries. In this paper, we review our recent works on the integrated optical signal processing system. We study three different kinds of on-chip signal processors and use these devices to build microsystems for the fields of microwave photonics, optical communications and spectrum sensing. The microwave photonics front receiver was demonstrated with a signal processing range of a full-band (L-band to W-band). A fully integrated microwave photonics transceiver without the on-chip laser was realized on silicon photonics covering the signal frequency of up 10 GHz. An all-optical orthogonal frequency division multiplexing (OFDM) de-multiplier was also demonstrated and used for an OFDM communication system with the rate of 64 Gbps. Finally, we show our work on the monolithic integrated spectrometer with a high resolution of about 20 pm at the central wavelength of 1550 nm. These proposed on-chip signal processing systems potential applications in the fields of radar, 5G wireless communication, wearable devices and optical access networks.

Conserved mechanism for coordinating replication fork helicase assembly with phosphorylation of the helicase

Dbf4-dependent kinase (DDK) phosphorylates minichromosome maintenance 2 (Mcm2) during S phase in yeast, and Sld3 recruits cell division cycle 45 (Cdc45) to minichromosome maintenance 2-7 (Mcm2-7). We show here DDK-phosphoryled Mcm2 preferentially interacts with Cdc45 in vivo, and that Sld3 stimulates DDK phosphorylation of Mcm2 by 11-fold. We identified a mutation of the replication initiation factor Sld3, Sld3-m16, that is specifically defective in stimulating DDK phosphorylation of Mcm2. Wild-type expression levels of sld3-m16 result in severe growth and DNA replication defects. Cells expressing sld3-m16 exhibit no detectable Mcm2 phosphorylation in vivo, reduced replication protein A-ChIP signal at an origin, and diminished Go, Ichi, Ni, and San association with Mcm2-7. Treslin, the human homolog of Sld3, stimulates human DDK phosphorylation of human Mcm2 by 15-fold. DDK phosphorylation of human Mcm2 decreases the affinity of Mcm5 for Mcm2, suggesting a potential mechanism for helicase ring opening. These data suggest a conserved mechanism for replication initiation: Sld3/Treslin coordinates Cdc45 recruitment to Mcm2-7 with DDK phosphorylation of Mcm2 during S phase.