Abstract
Bacterial actins polymerize in the presence of nucleotide (preferably ATP), form a common arrangement of monomeric interfaces within a protofilament, and undergo ATP hydrolysis-dependent change in stability of the filament—all of which contribute to performing their respective functions. The relative stability of the filament in the ADP-bound form compared to that of ATP and the rate of addition of monomers at the two ends decide the filament dynamics. One of the major differences between eukaryotic actin and bacterial actins is the variety in protofilament arrangements and dynamics exhibited by the latter. The filament structure and the polymerization dynamics enable them to perform various functions such as shape determination in rod-shaped bacteria (MreB), cell division (FtsA), plasmid segregation (ParM family of actin-like proteins), and organelle positioning (MamK). Though the architecture and dynamics of a few representative filaments have been studied, information on the effect of interacting partners on bacterial actin filament dynamics is not very well known. The chapter reviews some of the structural and functional aspects of bacterial actins, with special focus on the effect that interacting partners exert on the dynamics of bacterial actins, and how these assist them to carry out the functions within the bacterial cell.
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Acknowledgements
The work in the lab is supported by INSPIRE Faculty Research Grant, Department of Science and Technology (DST), Government of India, and Innovative Young Biotechnologist Award, Department of Biotechnology, Government of India, Extra Mural Research Grant from DST and IISER Pune.
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Gayathri, P. (2016). Bacterial Actins and Their Interactors. In: Mannherz, H. (eds) The Actin Cytoskeleton and Bacterial Infection. Current Topics in Microbiology and Immunology, vol 399. Springer, Cham. https://doi.org/10.1007/82_2016_31
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DOI: https://doi.org/10.1007/82_2016_31
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