Structural complexity of filaments formed from the actin and tubulin folds

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 mediu...

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Main Authors: Jiang, Shimin, Ghoshdastider, Umesh, Narita, Akihiro, Popp, David, Robinson, Robert Charles
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2018
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Online Access:https://hdl.handle.net/10356/89146
http://hdl.handle.net/10220/47022
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-891462020-11-01T05:26:34Z Structural complexity of filaments formed from the actin and tubulin folds Jiang, Shimin Ghoshdastider, Umesh Narita, Akihiro Popp, David Robinson, Robert Charles School of Biological Sciences Lee Kong Chian School of Medicine (LKCMedicine) NTU Institute of Structural Biology Actin Evolution DRNTU::Science::Medicine 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. Published version 2018-12-17T09:12:09Z 2019-12-06T17:18:54Z 2018-12-17T09:12:09Z 2019-12-06T17:18:54Z 2016 Journal Article 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 1942-0889 https://hdl.handle.net/10356/89146 http://hdl.handle.net/10220/47022 10.1080/19420889.2016.1242538 en Communicative & Integrative Biology © 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. 6 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Actin
Evolution
DRNTU::Science::Medicine
spellingShingle Actin
Evolution
DRNTU::Science::Medicine
Jiang, Shimin
Ghoshdastider, Umesh
Narita, Akihiro
Popp, David
Robinson, Robert Charles
Structural complexity of filaments formed from the actin and tubulin folds
description 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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Jiang, Shimin
Ghoshdastider, Umesh
Narita, Akihiro
Popp, David
Robinson, Robert Charles
format Article
author Jiang, Shimin
Ghoshdastider, Umesh
Narita, Akihiro
Popp, David
Robinson, Robert Charles
author_sort Jiang, Shimin
title Structural complexity of filaments formed from the actin and tubulin folds
title_short Structural complexity of filaments formed from the actin and tubulin folds
title_full Structural complexity of filaments formed from the actin and tubulin folds
title_fullStr Structural complexity of filaments formed from the actin and tubulin folds
title_full_unstemmed Structural complexity of filaments formed from the actin and tubulin folds
title_sort structural complexity of filaments formed from the actin and tubulin folds
publishDate 2018
url https://hdl.handle.net/10356/89146
http://hdl.handle.net/10220/47022
_version_ 1683494141759062016