Increasing Undergraduate Student Knowledge about Journal Peer Review Using Outside Reading and In-Class Discussion.

Peer review is an important part of the scientific publishing process that serves as a key quality control step. Learning that scientific publications go through peer review builds scientific literacy and may increase trust in published findings. Though the publication and peer review process is an established part of the practice of communicating science, this topic is not commonly taught at the undergraduate level, even in classes that regularly require students to read primary literature or author manuscripts.

Human CTP synthase filament structure reveals the active enzyme conformation.

The universally conserved enzyme CTP synthase (CTPS) forms filaments in bacteria and eukaryotes. In bacteria, polymerization inhibits CTPS activity and is required for nucleotide homeostasis. Here we show that for human CTPS, polymerization increases catalytic activity.

Large-scale filament formation inhibits the activity of CTP synthetase.

CTP Synthetase (CtpS) is a universally conserved and essential metabolic enzyme. While many enzymes form small oligomers, CtpS forms large-scale filamentous structures of unknown function in prokaryotes and eukaryotes. By simultaneously monitoring CtpS polymerization and enzymatic activity, we show that polymerization inhibits activity, and CtpS's product, CTP, induces assembly.

Self-assembling enzymes and the origins of the cytoskeleton.

The bacterial cytoskeleton is composed of a complex and diverse group of proteins that self-assemble into linear filaments. These filaments support and organize cellular architecture and provide a dynamic network controlling transport and localization within the cell. Here, we review recent discoveries related to a newly appreciated class of self-assembling proteins that expand our view of the bacterial cytoskeleton and provide potential explanations for its evolutionary origins.