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Current State of Microalgae-derived Biofuels and Bioproducts Research in South Korea: Outcome and Future Direction of Advanced Biomass R&D Center (ABC).

Medicinal Bioconvergence Research Center: An Integrated Research Platform for Novel Target and Lead Discovery.

BioNano Health Guard Research Center.

Bio-Synergy Research Center: Knowledge-based Systems Biology Platform for Natural Product Engineering.

Brief Introduction to the Project on Systems Metabolic Engineering for Biorefineries.

SINGAPORE – VIVA Foundation and NUS Launches $10 Million Cancer Research Centre for Childhood Leukaemia.

SINGAPORE – Discovery Paves the Way for Potential Genetics-Guided Precision Medicine for Paediatric Leukaemia Patients.

SINGAPORE – Partnership between Sony and Alder Hey Children's Hospital Drives Innovation in Children's Healthcare.

UNITED STATES – UGA Researchers Make Link between Genetics and Aging.

UNITED STATES – Latin Dancing may Have Health Benefits for Older Adults.

UNITED STATES – Interferon Not Beneficial for Most Stage III Melanoma.

UNITED STATES – Dissecting the Animal Diet, Past and Present.

UNITED STATES – Water Conservation Important to Many; Only Some Take Action.

UNITED KINGDOM – Innova Biosciences Introduces New LATEX One-Step Conjugation Kits.

UNITED KINGDOM – New Understanding of the Mechanism of Neurodegeneration Leads to a Novel Approach to Treatment for Alzheimer's Disease.

TAIWAN – Breakthrough in Homogeneous Antibody Development and a New Generation of Glycoarray Technology.

TAIWAN – Increasing Protein Synthesis by Leucine Ameliorates Synaptopathy Caused by Dementia, ALS and Autism.

Systematic studies have revealed that single gene deletions often display little phenotypic effects under laboratory conditions and that in many cases gene dispensability depends on the experimental conditions. To elucidate the environmental dependency of genes, we analyzed the effects of gene deletions by Phenotype MicroArray™ (PM), a system for quantitative screening of thousands of phenotypes in a high-throughput manner. Here, we proposed a new statistical approach to minimize error inherent in measurements of low respiration rates and find which mutants showed significant phenotypic changes in comparison to the wild-type. We show analyzing results from comprehensive PM assays of 298 single-gene knockout mutants in the Keio collection and two additional mutants under 1,920 different conditions. We focused on isozymes of these genes as simple duplications and analyzed correlations between phenotype changes and protein expression levels. Our results revealed divergence of the environmental dependency of the gene among the knockout genes and have also given some insights into possibilities of alternative pathways and availabilities of information on protein synthesis patterns to classify or predict functions of target genes from systematic phenotype screening.

Motivation: The synthesis of proteins with novel desired properties is challenging but sought after by the industry and academia. The dominating approach is based on trial-and-error inducing point mutations, assisted by structural information or predictive models built with paired data that are difficult to collect. This study proposes a sequence-based unpaired-sample of novel protein inventor (SUNI) to build ThermalProGAN for generating thermally stable proteins based on sequence information. Results: The ThermalProGAN can strongly mutate the input sequence with a median number of 32 residues. A known normal protein, 1RG0, was used to generate a thermally stable form by mutating 51 residues. After superimposing the two structures, high similarity is shown, indicating that the basic function would be conserved. Eighty four molecular dynamics simulation results of 1RG0 and the COVID-19 vaccine candidates with a total simulation time of 840ns indicate that the thermal stability increased. Conclusion: This proof of concept demonstrated that transfer of a desired protein property from one set of proteins is feasible.

Availability and implementation: The source code of ThermalProGAN can be freely accessed at https://github.com/markliou/ThermalProGAN/ with an MIT license.

The website is https://thermalprogan.markliou.tw:433.

Supplementary information: Supplementary data are available on Github.

The mTOR signaling cascade controls cell growth and metabolism and its deregulation underlies a variety of metabolic disorders. The mTOR pathway is characterized by two unique mTOR complexes: mTORC1 and mTORC2. mTORC1 is activated in the presence of nutrients to promote cell growth and proliferation while mTORC2 responds to nutrient fluctuations in order to restore metabolic homeostasis and maintain cell survival. Due to the pivotal role of the mTORCs in cell growth and survival, mTOR signaling is often upregulated in many cancers. mTOR is involved in many aspects of anabolic metabolism but the function of mTORC1 in protein synthesis is perhaps the most well studied. In this review, we will discuss how both mTORC1 and mTORC2 control protein synthesis. We begin with an in-depth analysis of the two multiprotein complexes and the specific upstream and downstream proteins involved in their signaling. In particular, we elaborate on how mTORC1 regulates translation via its targets S6K1 and 4E-BP1. We then discuss how both mTORC1 and mTORC2 could be involved in the regulation of other translation regulators such as RNA binding proteins and RSK, and elaborate on the role of mTOR in ribosome biogenesis. Finally, we review how mTOR also controls the processes that provide building blocks for protein synthesis including amino acids, ribose, and nucleotides. We also consider the role of mTOR in controlling catabolic processes such as autophagy and the ubiquitin proteasome system which are critical for providing intracellular nutrient sources as well as maintaining cellular proteostasis. This review provides a thorough background on how mTOR can function as a molecular rheostat to control global protein translation in response to nutrient availability.

High-resolution crystal structures of functionally active ribosomal particles provide unique tools for understanding key questions concerning ribosomal function, mobility, dynamics, and involvement in cellular regulation. Structure analysis of complexes of ribosomal particles with substrate analogs and universal drugs indicated that ribosomes provide the structural frame for precise positioning of the tRNA molecules rather than participate in the catalytic event, and that the peptide bond is being formed by a nucleophilic attack of the amino moiety of the residue bound to A-site tRNA on the carbonyl carbon at the P-site. Clinically relevant antibiotics interact almost exclusively with rRNA. They interfere with substrate binding, limit the conformational mobility, block the nascent chain exit tunnel or hinder the progression of growing peptide chains.

The analysis of protein synthesis has taken a leap due to the dramatic progress in crystallographic and cryo-EM studies of ribosomes and their subunits. To be able to understand the mechanisms involved in protein synthesis one has to consider the essential roles of the translation factors that catalyze different steps of the process. Most steps of protein synthesis are catalyzed by these factors. Of specific interest are the translational GTPases that undergo significant conformational changes associated with GTP hydrolysis. Two major questions are how is the GTPase activity induced and how does the conformational change induce the desired action in translation.

In the elongation cycle of translation, translocation is the process that advances the mRNA–tRNA moiety on the ribosome, to allow the next codon to move into the decoding center. New results obtained by cryoelectron microscopy, interpreted in the light of x-ray structures and kinetic data, allow us to develop a model of the molecular events during translocation.