Using knockouts of post translational modification enzymes to understand the role of tubulin post translational modifications on the motility and viability of Trypanosoma brucei

Abstract

Trypanosoma brucei is a pathogenic parasite that relies on a unique flagella bending waveform that alternates between base-to-tip and tip-to-base motility mechanisms for its virulence. The motile structure within the flagellum is the axoneme, which is composed of the canonical “9+2” arrangement of microtubules and axonemal dynein. Many accessory proteins, including dynein light and intermediate chains, directly regulate the mechanochemical cycle of dynein and flagellar motility. However, the impact of tubulin posttranslational modifications (PTMs) on the biophysical properties of dynein, such as binding affinity and velocity, remain largely unknown.