Membrane remodelling in bacteria

Bohuszewicz, Olga; Liu, Jiwei; Low, Harry H.

doi:10.1016/j.jsb.2016.05.010

Cited by 52 publications

(40 citation statements)

References 127 publications

(192 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, multiple paralogs distributed at distinct genomic locations or present as a tandem-pair/fused pair is not uncommon in bacteria [72,84,85]. It is recognized that the signature DSP domain architecture among the BDLPs is modified by deletions, fusion, and insertion of prokaryote-specific domains resulting in varied noncanonical forms that appear to have evolved to carry out divergent functional roles in membrane remodeling.…”

Section: Discussionmentioning

confidence: 99%

Molecular evolution of proteins mediating mitochondrial fission–fusion dynamics

Sinha

2019

FEBS Letters

View full text Add to dashboard Cite

Eukaryotes employ a subset of dynamins to mediate mitochondrial fusion and fission dynamics. Here we report the molecular evolution and diversification of the dynamin‐related mitochondrial proteins that drive the fission (Drp1) and the fusion processes (mitofusin and OPA1). We demonstrate that the three paralogs emerged concurrently in an early mitochondriate eukaryotic ancestor. Furthermore, multiple independent duplication events from an ancestral bifunctional fission protein gave rise to specialized fission proteins. The evolutionary history of these proteins is marked by transformations that include independent gain and loss events occurring at the levels of entire genes, specific functional domains, and intronic regions. The domain level variations primarily comprise loss–gain of lineage specific domains that are present in the terminal regions of the sequences.

show abstract

Section: Discussionmentioning

confidence: 99%

Molecular evolution of proteins mediating mitochondrial fission–fusion dynamics

Sinha

2019

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…Bacterial membrane extensions have been reported in multiple organisms: ‘Nanopods’ in Comamonadaceae including Delftia 31 , ‘outer membrane tubes’ in Francisella novicida 32 , ‘periplasmic tubules’ in Chlorochromatium aggregatum 33 , ‘ membrane tubules’ in Salmonella typhimurium 34 , ‘nanotubes’ connecting Escherichia coli cells to each other and to Acinetobacter baylyi cells 35 , and ‘connecting structures’ that allow exchange of material between Clostridium acetobutylicum and Desulfovibrio vulgaris cells 36 . However, membrane extensions in the form of OMV chains have only recently been discovered and much remains unknown about their formation mechanism and specific function 37 . In the Gram-negative Shewanella vesiculosa 38 and Myxococcus xanthus 39,40 and the Gram-positive Bacillus subtilis 41 , membrane extensions in the form of OMV chains, similar to those reported here, have been observed using cryo-EM with implications for cell-cell connections in the latter two examples.…”

Section: Discussionmentioning

confidence: 99%

The ultrastructure ofShewanella oneidensisMR-1 nanowires revealed by electron cryo-tomography

Subramanian¹,

Pirbadian

El‐Naggar

et al. 2017

Preprint

View full text Add to dashboard Cite

nanowires are extensions of the outer membrane that contain EET components. 6However, their fine structure and distribution of cytochrome electron carriers 2 7 remained unclear, making it difficult to evaluate the electron transport mechanism 2 8 along the nanowires. Here, we report high-resolution images of nanowires using 2 9Electron Cryo-Tomography (ECT). We developed a robust method for fLM 3 0 imaging of nanowire growth on electron microscopy grids and used correlative 3 1 light and electron microscopy to identify and image the same nanowires by ECT. proteins consistent with cytochromes. We observe tight packing of putative 3 9 cytochromes along lateral patches that extend tens of nanometers, but not across 4 0

show abstract

mentioning

confidence: 99%

“…They share a conserved domain architecture with the canonical human Dynamin 1, including the N-terminal GTPase domain, a neck domain involved in dynamin dimerization, and a trunk domain involved in stimulation of GTPase activity (4,5). In contrast, bacterial dynamins lack the pleckstrin homology motif and proline-rich sequences found in classical dynamins and contain instead other lipidand protein-binding motifs (5). Structural and biochemical studies on Nostoc punctiforme BLDP1, Bacillus subtilis DynA, and Escherichia coli LeoA have provided clear insight into the mechanism of protein oligomerization and lipid binding (2,3,6,7), but unlike those of their eukaryotic counterparts the biological functions of bacterial dynamins have remained largely unclear.…”

mentioning

confidence: 99%

Two dynamin-like proteins stabilize FtsZ rings during Streptomyces sporulation

Schlimpert

Wasserström

Chandra

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

During sporulation, the filamentous bacteria Streptomyces undergo a massive cell division event in which the synthesis of ladders of sporulation septa convert multigenomic hyphae into chains of unigenomic spores. This process requires cytokinetic Z-rings formed by the bacterial tubulin homolog FtsZ, and the stabilization of the newly formed Z-rings is crucial for completion of septum synthesis. Here we show that two dynamin-like proteins, DynA and DynB, play critical roles in this process. Dynamins are a family of large, multidomain GTPases involved in key cellular processes in eukaryotes, including vesicle trafficking and organelle division. Many bacterial genomes encode dynamin-like proteins, but the biological function of these proteins has remained largely enigmatic. Using a cell biological approach, we show that the two Streptomyces dynamins specifically localize to sporulation septa in an FtsZ-dependent manner. Moreover, dynamin mutants have a cell division defect due to the decreased stability of sporulation-specific Z-rings, as demonstrated by kymographs derived from time-lapse images of FtsZ ladder formation. This defect causes the premature disassembly of individual Z-rings, leading to the frequent abortion of septum synthesis, which in turn results in the production of long spore-like compartments with multiple chromosomes. Two-hybrid analysis revealed that the dynamins are part of the cell division machinery and that they mediate their effects on Z-ring stability during developmentally controlled cell division via a network of protein-protein interactions involving DynA, DynB, FtsZ, SepF, SepF2, and the FtsZ-positioning protein SsgB.he active organization and remodeling of cellular membranes is a fundamental process for all organisms. Many of these remodeling events involve the reshaping, fission, or fusion of lipid bilayers to generate new organelles, release transport vesicles, or stabilize specific membrane structures. In eukaryotes, key cellular processes, such as the fission and fusion of mitochondria, the division of chloroplasts, endocytosis, and viral resistance, are mediated by members of the dynamin superfamily (1). Dynamins and dynamin-like proteins are mechanochemical GTPases that polymerize into helical scaffolds at the surface of membranes. GTP hydrolysis is coupled to a radical conformational change in the protein structure that forces the underlying lipid layer into an energetically unstable conformation that promotes membrane rearrangements, probably via a hemifusion intermediate (2, 3).Dynamin-like proteins are found in many bacterial species, yet the precise roles of these proteins are still largely unknown. They share a conserved domain architecture with the canonical human Dynamin 1, including the N-terminal GTPase domain, a neck domain involved in dynamin dimerization, and a trunk domain involved in stimulation of GTPase activity (4, 5). In contrast, bacterial dynamins lack the pleckstrin homology motif and proline-rich sequences found in classical dynamins and contain instead o...

show abstract

Membrane remodelling in bacteria

Cited by 52 publications

References 127 publications

Molecular evolution of proteins mediating mitochondrial fission–fusion dynamics

Molecular evolution of proteins mediating mitochondrial fission–fusion dynamics

The ultrastructure ofShewanella oneidensisMR-1 nanowires revealed by electron cryo-tomography

Two dynamin-like proteins stabilize FtsZ rings during Streptomyces sporulation

Contact Info

Product

Resources

About