Novel Actin-like Filament Structure from Clostridium tetani

Popp, David; Narita, Akihiro; Lee, Lin Jie; Ghoshdastider, Umesh; Xue, Bin; Srinivasan, R.; Balasubramanian, Mohan K.; Tanaka, Takehide; Robinson, Robert

doi:10.1074/jbc.m112.341016

Cited by 33 publications

(31 citation statements)

References 37 publications

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“…In other cases (i.e. PDBid: 4APW), grown filaments may interact between themselves in opposite polarities (shown for example [17]). But what about those more complex protein assemblies in which the total hydrophobic moment is not canceled by a similar one opposing it?…”

Section: Discussionmentioning

confidence: 99%

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Self-Assembly of Open Protein Systems: A Comprehensive View Based onthe Interactions between 3d Hydrophobic and Electric Dipole MomentVectors

Mozo-Villarías¹,

Cedano²,

Querol³

2017

J Proteomics Bioinform

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Section: Discussionmentioning

confidence: 99%

“…For a 3D visualization using UCSD Chimera, visit http://wallace.uab.es/Self-assembling/ (see Methods). b) Actin, PDBid: 4APW [17]. The basic element for growth is monomeric prokaryotic actin.…”

Section: Amyloid and Stacking Assemblymentioning

confidence: 99%

Self-Assembly of Open Protein Systems: A Comprehensive View Based onthe Interactions between 3d Hydrophobic and Electric Dipole MomentVectors

Mozo-Villarías¹,

Cedano²,

Querol³

2017

J Proteomics Bioinform

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“…These highly divergent ParM amino acid sequences ( Fig. 1) have recently been shown to translate into equally divergent filament architectures (Gayathri et al, 2013;Popp et al, 2010a;Popp et al, 2012;Popp et al, 2010b), which adds some weight to the hypothesis that an element of positive selection to diverge might have existed between selected ParMs.…”

Section: Bacterial Actinsmentioning

confidence: 94%

The evolution of compositionally and functionally distinct actin filaments

Gunning

Ghoshdastider

Whitaker

et al. 2015

Journal of Cell Science

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261

198

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The actin filament is astonishingly well conserved across a diverse set of eukaryotic species. It has essentially remained unchanged in the billion years that separate yeast, Arabidopsis and man. In contrast, bacterial actin-like proteins have diverged to the extreme, and many of them are not readily identified from sequence-based homology searches. Here, we present phylogenetic analyses that point to an evolutionary drive to diversify actin filament composition across kingdoms. Bacteria use a one-filament-one-function system to create distinct filament systems within a single cell. In contrast, eukaryotic actin is a universal force provider in a wide range of processes. In plants, there has been an expansion of the number of closely related actin genes, whereas in fungi and metazoa diversification in tropomyosins has increased the compositional variety in actin filament systems. Both mechanisms dictate the subset of actin-binding proteins that interact with each filament type, leading to specialization in function. In this Hypothesis, we thus propose that different mechanisms were selected in bacteria, plants and metazoa, which achieved actin filament compositional variation leading to the expansion of their functional diversity.

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“…Similar to ParM, both proteins assemble into filaments in the presence ATP or GTP and Mg 2+ , but the architecture and ultrastructure of these filaments is different 20-22 . AlfA filaments have a strong propensity to form bundles in vitro .…”

Section: Parm and Other Plasmid Segregating Bacterial Actinsmentioning

confidence: 99%

Bacterial Actins and Their Diversity

2013

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For many years bacteria were considered rather simple organisms, but the dogmatic notion that subcellular organization is a eukaryotic trait has been overthrown for more than a decade. The discovery of homologs of the eukaryotic cytoskeletal proteins actin, tubulin, and intermediate filaments in bacteria has been instrumental in changing this view. Over the recent years we gained an incredible level of insight into the diverse family of bacterial actins and their molecular workings. Here we review the functional, biochemical and structural features of the most well-studied bacterial actins.

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Novel Actin-like Filament Structure from Clostridium tetani

Cited by 33 publications

References 37 publications

Self-Assembly of Open Protein Systems: A Comprehensive View Based onthe Interactions between 3d Hydrophobic and Electric Dipole MomentVectors

Self-Assembly of Open Protein Systems: A Comprehensive View Based onthe Interactions between 3d Hydrophobic and Electric Dipole MomentVectors

The evolution of compositionally and functionally distinct actin filaments

Bacterial Actins and Their Diversity

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