Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/89146
Title: Structural complexity of filaments formed from the actin and tubulin folds
Authors: Jiang, Shimin
Ghoshdastider, Umesh
Narita, Akihiro
Popp, David
Robinson, Robert Charles
Keywords: Actin
Evolution
DRNTU::Science::Medicine
Issue Date: 2016
Source: Jiang, S., Ghoshdastider, U., Narita, A., Popp, D., & Robinson, R. C. (2016). Structural complexity of filaments formed from the actin and tubulin folds. Communicative & Integrative Biology, 9(6), e1242538-. doi:10.1080/19420889.2016.1242538
Series/Report no.: Communicative & Integrative Biology
Abstract: From yeast to man, an evolutionary distance of 1.3 billion years, the F-actin filament structure has been conserved largely in line with the 94% sequence identity. The situation is entirely different in bacteria. In comparison to eukaryotic actins, the bacterial actin-like proteins (ALPs) show medium to low levels of sequence identity. This is extreme in the case of the ParM family of proteins, which often display less than 20% identity. ParMs are plasmid segregation proteins that form the polymerizing motors that propel pairs of plasmids to the extremities of a cell prior to cell division, ensuring faithful inheritance of the plasmid. Recently, exotic ParM filament structures have been elucidated that show ParM filament geometries are not limited to the standard polar pair of strands typified by actin. Four-stranded non-polar ParM filaments existing as open or closed nanotubules are found in Clostridium tetani and Bacillus thuringiensis, respectively. These diverse architectures indicate that the actin fold is capable of forming a large variety of filament morphologies, and that the conception of the “actin” filament has been heavily influenced by its conservation in eukaryotes. Here, we review the history of the structure determination of the eukaryotic actin filament to give a sense of context for the discovery of the new ParM filament structures. We describe the novel ParM geometries and predict that even more complex actin-like filaments may exist in bacteria. Finally, we compare the architectures of filaments arising from the actin and tubulin folds and conclude that the basic units possess similar properties that can each form a range of structures. Thus, the use of the actin fold in microfilaments and the tubulin fold for microtubules likely arose from a wider range of filament possibilities, but became entrenched as those architectures in early eukaryotes.
URI: https://hdl.handle.net/10356/89146
http://hdl.handle.net/10220/47022
ISSN: 1942-0889
DOI: 10.1080/19420889.2016.1242538
Rights: © 2016 Shimin Jiang, Umesh Ghoshdastider, Akihiro Narita, David Popp, and Robert C. Robinson. Published with license by Taylor & Francis. This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles

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