Research
Bacterial cytoskeleton and interacting proteins in polarity oscillations and chemotaxis
Myxococcus xanthus undergoes cell polarity oscillations in response to environmental cues during its motility. Hence, it serves as an ideal system for understanding active processes of localization of macromolecular complexes within the cell upon sensing an environmental signal.
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Demonstration of GAP-only activity of MglB on another small Ras-like GTPase SofG. Kanade, et al., FEBS J 2020
Characterization of a prokaryotic small Ras-like GTPase MglA and its regulator MglB led to the identification of a novel allosteric mechanism for GTPase activity. MglB functions both as a GAP and GEF. Baranwal, et al., PLOS Biology 2019
Discovery of a unique DNA binding property for the cytoplasmic methyl accepting chemosensory protein (MCP) FrzCD. Moine et al., PLOS Genetics 2017
Interfilament interactions of the bacterial cytoskeleton in shape determination and motility
Spiroplasma is a helical cell wall-less bacterium. Current models on cell shape determination of cell-walled bacteria propose a mechanism based on interplay of cytoskeleton and cell wall synthesis machinery. Spiroplasma possesses a distinct shape and prominent number of cytoskeletal proteins (5 paralogs of bacterial actin MreB, a cytoskeletal protein of novel fold Fibril, FtsZ and FtsA). Hence it serves as an ideal model system for understanding cytoskeleton-driven mechanism of cell shape determination, cell division and motility.
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Demonstration of the direct role of MreB5 in helical shape determination. Harne, et al., Curr Biol 2020
Sequence and structural analysis of nucleotide-binding proteins
Research highlights:
Analysis of myosin motor domain has led to the structural basis for defective function of many myosin mutations identified during genetic experiments in fission yeast. Palani, et al., Curr Biol 2017; Palani, et al., J Cell Sci 2018; Zambon, et al., MBoC 2020
Identification of a novel Walker B motif in prokaryotic GTPases. Kanade, et al., JMB 2020
Tools
Structural biology (X-ray crystallography and electron cryomicroscopy), biochemical and biophysical tools and fluorescence microscopy are used to capture the structure and dynamics of macromolecular assemblies at both spatial and temporal resolutions.