Conservation Analysis of Myosin Families

Abstract

Myosins are involved in many cellular tasks, including organelle trafficking, cytokinesis, maintenance of cell shape, and muscle contraction. Different myosins perform different tasks with distinct mechanical and chemical characteristics. Although their core structures are similar, their subtle differences in sequence can cause drastic differences in these characteristics. This study used sequence analysis to identify conserved and unique structures of several myosin families including myosin II, myosin V, and myosin VI. Using myosin VI as an example, we identified several myosin VI-specific residues where all myosin VI proteins have an identical amino acid but no other myosin has the same amino acid in the same aligned column. P444 may contributes to the weaker binding to actin in myosin VI comparing to myosin II and V. M701 is located at the tip of SH1 helix which is the linkage between motor domain and converter. F763 is located in the converter which strongly interacts with the motor domain to position the converter. This method can also be applied to other myosin families to gain mechanistic understanding of myosin functions.