Bacterial Cytoskeleton in Motility and Shape

                                                       Research Overview

Cytoskeletal assemblies of protein molecules play a pivotal role in vital functions of the cell such as shape determination, motility, cell division and active positioning of molecules within the cell. Major classes of cytoskeletal proteins in eukaryotes are actin, tubulin and intermediate filaments. These filamentous assemblies and associated proteins such as molecular motors (eg. myosin, dynein and kinesin) and small Ras-like GTPases are well characterized in eukaryotes.

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A variety of prokaryotic equivalents of actin and tubulin have been identified. However, very few proteins associated with the bacterial cytoskeleton and their functions have been characterized. Bacteria also possess novel cytoskeletal filaments other than of actin or tubulin fold, with unknown function. Since molecular motors such as myosin, dynein and kinesin have not been identified by sequence-based searches, the functional equivalents of these cytoskeleton-associated molecular motors in prokaryotes remain elusive.

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In order to understand the functional equivalents of cytoskeleton-associated molecular motors in bacteria, the work in my group focuses on the mechanistic basis of biological processes typically performed by molecular motors in eukaryotes. With this goal, we study the molecular basis of cytoskeleton-based shape determination and motility.