Abstract

Bioinformatics Genome-Wide Survey of Myosins

R Sowdhamini, Professor, NCBS

Myosins control many fundamental dynamic organizations of cellular components. Different biological functions within this large family of molecular motors depend on differences in their tail domains, especially the region that is rich in the a-helical coiled coil motif. While regions that deviate from a strong coiled coil motif are common, they have been largely ignored in structure-function studies. In a collaborative effort with Prof. Jim Spudich of Stanford and Prof. Henrik Flyvbjerg of Copenhagen, we have carried out detailed bioinformatics and biophysical analysis of myosins. We have created tools for the structural analysis of coiled coils such that structural deviations within the tail domains of the myosin family can be examined. We have also studied the structural deviations from an evolutionary perspective by comparing types of myosins across different genomes. These are presented as an user friendly Myosinome database. We have implored into the larger dataset of sequences in the superkingdom of life to identify newer myosin families. We also propose and reveal the important roles of the myosin tail domains, such as protein-protein interactions and structural switch points, along with their interacting partners. Such studies should shed light on the structure and function of this important family of enzymes.