Viral Capsid Trafficking along Treadmilling Tubulin Filaments in Bacteria

Chaikeeratisak, Vorrapon; Khanna, K. N.; Nguyen, Katrina; Sugie, Joseph; Egan, MacKennon E.; Erb, Marcella L.; Vavilina, Anastasia; Nonejuie, Poochit; Nieweglowska, Eliza S.; Pogliano, Kit; Agard, David A.; Villa, Elizabeth; Pogliano, Joe

doi:10.1016/j.cell.2019.05.032

Cited by 74 publications

(149 citation statements)

References 34 publications

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“…Fluorescence recovery after photobleaching (FRAP) demonstrated that normal PhuZ spindles treadmill (Fig. 3b , left; 16 ), while the hybrid spindles were not dynamic (Fig. 3b , right).…”

Section: Resultsmentioning

confidence: 99%

Viral speciation through subcellular genetic isolation and virogenesis incompatibility

et al. 2021

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Understanding how biological species arise is critical for understanding the evolution of life on Earth. Bioinformatic analyses have recently revealed that viruses, like multicellular life, form reproductively isolated biological species. Viruses are known to share high rates of genetic exchange, so how do they evolve genetic isolation? Here, we evaluate two related bacteriophages and describe three factors that limit genetic exchange between them: 1) A nucleus-like compartment that physically separates replicating phage genomes, thereby limiting inter-phage recombination during co-infection; 2) A tubulin-based spindle that orchestrates phage replication and forms nonfunctional hybrid polymers; and 3) A nuclear incompatibility factor that reduces phage fitness. Together, these traits maintain species differences through Subcellular Genetic Isolation where viral genomes are physically separated during co-infection, and Virogenesis Incompatibility in which the interaction of cross-species components interferes with viral production.

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“…Fluorescence recovery after photobleaching (FRAP) demonstrated that normal PhuZ spindles treadmill (Fig. 3b , left; 16 ), while the hybrid spindles were not dynamic (Fig. 3b , right).…”

Section: Resultsmentioning

confidence: 99%

Viral speciation through subcellular genetic isolation and virogenesis incompatibility

et al. 2021

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“…These viruses encode a distant homologue of the eukaryotic tubulin that localizes this nucleus-like structure in the middle of the virocell (i.e. the virus-infected cell) and treadmills toward it the viral capsids that were assembled on the membrane 26 . It is possible that viractins play a similar role during viral infections by controlling the localization of the viral factory close to the host nucleus (e.g., as seen in Yasminevirus 6 ).…”

Section: Discussionmentioning

confidence: 99%

Giant viruses encode novel types of actins possibly related to the origin of eukaryotic actin: the viractins

Gaïa

Ogata

et al. 2020

Preprint

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Actin is a major component of the eukaryotic cytoskeleton. Many related actin homologues can be found in eukaryotes1, some of them being present in most or all eukaryotic lineages. The gene repertoire of the Last Eukaryotic Common Ancestor (LECA) therefore would have harbored both actin and various actin-related proteins (ARPs). A current hypothesis is that the different ARPs originated by gene duplication in the proto-eukaryotic lineage from an actin gene that was inherited from Asgard archaea. Here, we report the first detection of actin-related genes in viruses (viractins), encoded by 19 genomes belonging to the Imitervirales, a viral order encompassing the giant Mimiviridae. Most viractins were closely related to the actin, contrasting with actin-related genes of Asgard archaea and Bathyarchaea (a newly discovered clade). Our phylogenetic analysis suggests viractins could have been acquired from proto-eukaryotes and possibly gave rise to the conventional eukaryotic actin after being reintroduced into the pre-LECA eukaryotic lineage.

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“…( 55 ). The filament-forming phage tubulin PhuZ ( 56 ) and its roles in the spatial organization of large phage DNA and directed movements of capsids in the cells have been demonstrated ( 57 , 58 ).…”

Section: Discussionmentioning

confidence: 99%

Unique Properties of the Alpha-Helical DNA-Binding Protein KfrA Encoded by the IncU Incompatibility Group Plasmid RA3 and Its Host-Dependent Role in Plasmid Maintenance

Lewicka

Mitura

Steczkiewicz

et al. 2021

Appl Environ Microbiol

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KfrA of the broad host range RA3 plasmid is an alpha-helical DNA-binding protein that acts as a transcriptional autoregulator. KfrARA3 operator site overlaps the kfrA promoter and is composed of five 9 bp repeats (DR). Here, the biological properties of KfrA were studied using both in vivo and in vitro approaches. Localization of DNA binding helix-turn-helix motif (HTH) was mapped to the N29-R52 region by protein structure modelling and confirmed by the alanine scanning. KfrA repressor ability depended on the number and orientation of DRs in the operator, as well as the ability of the protein to oligomerize. Long alpha-helical tail of residues 54-355, was shown to be involved in the self-interactions whereas 54-177 region was involved in heterodimerization with KfrC, another RA3 encoded alpha-helical protein. KfrA also interacted with the segrosome proteins, IncC (ParA) and KorB (ParB), representatives of the class Ia active partition systems. Deletion of the kfr genes from the RA3 stability module decreased the plasmid retention in diverse hosts in a species-dependent manner. The specific interactions of KfrA with DNA are essential not only for the transcriptional regulatory function but also for the accessory role of KfrA in the plasmid stable maintenance. Importance Alpha-helical coiled-coil KfrA-type proteins are encoded by various broad-host-range low copy number conjugative plasmids. DNA-binding KfrA protein of the RA3 plasmid from IncU incompatibility group oligomerizes, forms a complex with another plasmid-encoded, alpha-helical protein, KfrC and interacts with the segrosome proteins IncC and KorB. The unique mode of KfrA dimer binding to the repetitive operator is required for a KfrA role in the stable maintenance of RA3 plasmid in distinct hosts.

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Viral Capsid Trafficking along Treadmilling Tubulin Filaments in Bacteria

Abstract: Highlights d Capsids traffic along a viral encoded tubulin filament d Treadmilling of the filament provides the mechanism of capsid movement through the cell d Rotation of phage nucleus by the filament distributes capsids for efficient DNA packaging

Cited by 74 publications

References 34 publications

Viral speciation through subcellular genetic isolation and virogenesis incompatibility

Viral speciation through subcellular genetic isolation and virogenesis incompatibility

Giant viruses encode novel types of actins possibly related to the origin of eukaryotic actin: the viractins

Unique Properties of the Alpha-Helical DNA-Binding Protein KfrA Encoded by the IncU Incompatibility Group Plasmid RA3 and Its Host-Dependent Role in Plasmid Maintenance

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