Electron handoff

May 16th, 2018 by Caitlin Deane

Electron handoff

Electron handoff, Published online: 16 May 2018; doi:10.1038/s41589-018-0073-9

Electron handoff

Membrane association of monotopic phosphoglycosyl transferase underpins function

May 16th, 2018 by Leah C. Ray

Membrane association of monotopic phosphoglycosyl transferase underpins function

Membrane association of monotopic phosphoglycosyl transferase underpins function, Published online: 16 May 2018; doi:10.1038/s41589-018-0054-z

The structure of a monotopic polyprenol phosphate phosphoglycosyl transferase, PglC, reveals how it interacts with the bacterial membrane and coordinates a reaction between membrane-embedded and soluble substrates during glycoconjugate assembly.
  • Posted in Nat Chem Biol, Publications
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tRNA tracking for direct measurements of protein synthesis kinetics in live cells

May 16th, 2018 by Ivan L. Volkov

tRNA tracking for direct measurements of protein synthesis kinetics in live cells

tRNA tracking for direct measurements of protein synthesis kinetics in live cells, Published online: 16 May 2018; doi:10.1038/s41589-018-0063-y

Combination of single-molecule tracking experiments and machine-learning approaches to monitor diffusional state transitions between ribosome-bound and free tRNAs allows codon resolution measurements of translation kinetics.
  • Posted in Nat Chem Biol, Publications
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Next-generation biocontainment systems for engineered organisms

May 16th, 2018 by Jeong Wook Lee

Next-generation biocontainment systems for engineered organisms

Next-generation biocontainment systems for engineered organisms, Published online: 16 May 2018; doi:10.1038/s41589-018-0056-x

Synthetic biology offers innovative approaches for engineering biological systems, but also supports the development of biocontainment strategies that ensure the safe application of genetically modified organisms.

Identification of a <i>S. aureus</i> virulence factor by activity-based protein profiling (ABPP)

May 16th, 2018 by Christian S. Lentz

Identification of a S. aureus virulence factor by activity-based protein profiling (ABPP)

Identification of a <i>S. aureus</i> virulence factor by activity-based protein profiling (ABPP), Published online: 16 May 2018; doi:10.1038/s41589-018-0060-1

ABP profiling identifies uncharacterized S. aureus serine hydrolases, including the surface-localized FphB, which processes lipid ester substrates and is required for infection in vivo. An FphB inhibitor reduces in vivo bacterial load.
  • Posted in Nat Chem Biol, Publications
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Functional phosphorylation

May 16th, 2018 by Mirella Bucci

Functional phosphorylation

Functional phosphorylation, Published online: 16 May 2018; doi:10.1038/s41589-018-0075-7

Functional phosphorylation

[ASAP] Drug-Inducible Control of Lethality Genes: A Low Background Destabilizing Domain Architecture Applied to the Gal4-UAS System in <italic toggle=”yes”>Drosophila</italic>

May 14th, 2018 by Manjunatha Kogenaru, Mark Isalan

TOC Graphic

ACS Synthetic Biology
DOI: 10.1021/acssynbio.7b00302
  • Posted in ACS Synthetic Biology, Publications
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[ASAP] A Dynamic Model of Resource Allocation in Response to the Presence of a Synthetic Construct

May 9th, 2018 by Axel Nyström, Antonis Papachristodoulou, Andrew Angel

TOC Graphic

ACS Synthetic Biology
DOI: 10.1021/acssynbio.8b00015

The ribosome: A hot spot for the identification of new types of protein methyltransferases [Protein Synthesis and Degradation]

May 9th, 2018 by Steven G. Clarke

Cellular physiology depends on the alteration of protein structures by covalent modification reactions. Using a combination of bioinformatic, genetic, biochemical, and mass spectrometric approaches, it has been possible to probe ribosomal proteins from the yeast Saccharomyces cerevisiae for posttranslationally methylated amino acid residues and for the enzymes that catalyze these modifications. These efforts have resulted in the identification and characterization of the first protein histidine methyltransferase, the first N-terminal protein methyltransferase, two unusual types of protein arginine methyltransferases, and a new type of cysteine methylation. Two of these enzymes may modify their substrates during ribosomal assembly because the final methylated histidine and arginine residues are buried deep within the ribosome with contacts only with RNA. Two of these modifications occur broadly in eukaryotes, including humans, while the others demonstrate a more limited phylogenetic range. Analysis of strains where the methyltransferase genes are deleted has given insight into the physiological roles of these modifications. These reactions described here add diversity to the modifications that generate the typical methylated lysine and arginine residues previously described in histones and other proteins.

Lessons from my undergraduate research students [Computational Biology]

May 9th, 2018 by Paul A Craig

From very early on, my personal/professional life has been shaped by teachers in many different settings. Teaching and learning form a two-way street. In the process of teaching undergraduate students, particularly in the research lab, I have learned some profound lessons about the importance of listening to them, challenging them, giving them autonomy, and allowing them to enjoy success and risk failure. I am now working with a team of faculty members to implement these lessons in a course-based undergraduate research experience in the biochemistry teaching lab. Our goal is to seek answers to the question, "How do students become scientists?" and to implement those answers with our future students.