Yin-Wei Kuo

Abstract The homology of the archaeal and eukaryotic ribosome provides one of the key pieces of evidence that underpins the idea that eukaryotes acquired their core information processing machinery from archaea. Since this discovery, reverse genetics has been used to study the functions of many archaeal proteins with eukaryotic homologues.

Abstract The control of biopolymer length is mediated by proteins that localize to polymer ends and regulate polymerization dynamics. Several mechanisms have been proposed to achieve end localization. Here, we propose a novel mechanism by which a protein that binds to a shrinking polymer and slows its shrinkage will be spontaneously enriched at the shrinking end through a “herding” effect.

Introduction Microtubules, essential components of the eukaryotic cytoskeleton, are cylindrical filaments made up of typically 13 protofilaments. They are highly dynamic polymers that stochastically switch between phases of slow growth and fast shrinkage ( 1 Mitchison T. Kirschner M. Dynamic instability of microtubule growth. ). The switch from growth to shrinkage is termed catastrophe and is thought to be due to the loss of a cap of GTP-tubulin at the growing end ( 2 Kirschner M. Mitchison T.