Inari Kursula lab

Check out our latest myosin work!

Isa's work on Plasmodium falciparum myosin B is out on the preprint server bioRxiv - just in time for her PhD defense. Hopefully soon in peer-reviewed form too.

QR code to the preprint
Inari Kursula

Main content

In this paper, we describe the expression and purification of the smallest of the malaria parasite myosins, MyoB, in complex with the calmodulin-like domain of its known light chain MLC-B. We characterized the complex using small-angle X-ray scattering, circular dichroism spectroscopy, and biochemical assays to determine the kinetics of the MyoB ATPase cycle. The complex has an overall shape of a monomeric myosin motor domain. The MyoB neck region can bind to several other regulatory light chains, in addition to MLC-B. However, we could not identify any essential light chain that would bind to the first IQ domain of the MyoB neck - either in the presence or absence of MLC-B. The recombinant MyoB moved actin filaments in vitro, and its ADP release rate was faster than the ATP turnover. MyoB has a much higher affinity to actin than the other small class XIV myosin of the parasite, MyoA. This supports a role in tethering and/or force sensing during early stages of invasion, where MyoB is strictly localized to the apical end of the parasite.

Scan the QR code or click here!