Prokaryotic cells: structural organisation of the cytoskeleton and organelles

Souza, Wanderley de

doi:10.1590/s0074-02762012000300001

Cited by 7 publications

(2 citation statements)

References 109 publications

(96 reference statements)

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“…FtsZ tubulin diverged from a common ancestor early in evolution, whereas BtubA/B likely split from eukaryotic tubulin more recently. Their structural and organizational features have been reviewed [Souza, 2012], but the functions of BtuBa and BtubB are unknown.…”

Section: The Bacterial Cytoskeletonmentioning

confidence: 99%

“…The protein has biochemical properties and a domain structure similar to those of eukaryotic IFs. Crescentin localizes to the concave side of the bacterium along its inner surface, associating with the cell membrane [Souza, 2012]. Coiled coil-rich proteins are also required for the maintenance of helical cell shape in the human pathogen Helicobacter pylori [Waidner et al, 2009], revealing a conserved function for this type of proteins.…”

Section: The Bacterial Cytoskeletonmentioning

confidence: 99%

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Microcompartments and Protein Machines in Prokaryotes

Saier

2013

Microb Physiol

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The prokaryotic cell was once thought of as a ‘bag of enzymes' with little or no intracellular compartmentalization. In this view, most reactions essential for life occurred as a consequence of random molecular collisions involving substrates, cofactors and cytoplasmic enzymes. Our current conception of a prokaryote is far from this view. We now consider a bacterium or an archaeon as a highly structured, nonrandom collection of functional membrane-embedded and proteinaceous molecular machines, each of which serves a specialized function. In this article we shall present an overview of such microcompartments including (1) the bacterial cytoskeleton and the apparati allowing DNA segregation during cell division; (2) energy transduction apparati involving light-driven proton pumping and ion gradient-driven ATP synthesis; (3) prokaryotic motility and taxis machines that mediate cell movements in response to gradients of chemicals and physical forces; (4) machines of protein folding, secretion and degradation; (5) metabolosomes carrying out specific chemical reactions; (6) 24-hour clocks allowing bacteria to coordinate their metabolic activities with the daily solar cycle, and (7) proteinaceous membrane compartmentalized structures such as sulfur granules and gas vacuoles. Membrane-bound prokaryotic organelles were considered in a recent Journal of Molecular Microbiology and Biotechnology written symposium concerned with membranous compartmentalization in bacteria [J Mol Microbiol Biotechnol 2013;23:1-192]. By contrast, in this symposium, we focus on proteinaceous microcompartments. These two symposia, taken together, provide the interested reader with an objective view of the remarkable complexity of what was once thought of as a simple noncompartmentalized cell.

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Section: The Bacterial Cytoskeletonmentioning

confidence: 99%

Section: The Bacterial Cytoskeletonmentioning

confidence: 99%

Microcompartments and Protein Machines in Prokaryotes

Saier

2013

Microb Physiol

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Molecular association of FtsZ with the intrabacterial nanotransportation system for urease in Helicobacter pylori

Iwai

Suzuki

et al. 2019

Med Mol Morphol

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Prokaryotic cytoskeletons: in situ and ex situ structures and cellular locations

Kim

2018

Antonie van Leeuwenhoek

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Cytoskeletons have long been perceived to be present only in eukaryotes. However, this notion changed drastically in the 1990s, with observations of cytoskeleton-like structures in several prokaryotes. Homologs of the main components of eukaryotic cytoskeletons, such as microtubules, microfilaments, and intermediate filaments, have been identified in bacteria and archaea. Tubulin homologs include filamenting temperature-sensitive mutant Z (FtsZ), bacterial tubulin A/B (BtubA/B), and tubulin/FtsZ-like protein (TubZ), whereas actin homologs comprise murein region B (MreB) and crenactin. Unlike other proteins, crescentin (CreS) is a homolog of intermediate filaments. Recent findings elucidated their localization, structural organization, and helical properties in prokaryotes, thus revising traditional models. FtsZ is involved in cell division, forming a bundle of overlapping filaments that cover the entire division plane. Cryogenic transmission electron microscopy identified tubular structures of BtubA/B that were not previously identified using conventional ultrathin plastic sections. TubZ generates two joint filaments to form a quadruplex structure. After a long debate, MreB, a cell shape determinant, was shown to form filament stretches that move circumferentially around rod-shaped bacteria. Initially characterized as single-stranded, crenactin was eventually identified as right-handed double-stranded helical filaments. CreS, another cell shape determinant, forms filament bundles located inside the inner membrane of the concave side of cells. These observations suggest that the use of in situ or ex situ microscopy in combination with structural analysis techniques will enable the elucidation and further understanding of the current models of prokaryotic cytoskeletons.

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Prokaryotic cells: structural organisation of the cytoskeleton and organelles

Cited by 7 publications

References 109 publications

Microcompartments and Protein Machines in Prokaryotes

Microcompartments and Protein Machines in Prokaryotes

Molecular association of FtsZ with the intrabacterial nanotransportation system for urease in Helicobacter pylori

Prokaryotic cytoskeletons: in situ and ex situ structures and cellular locations

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