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The prokaryotic cytoskeletal elements are matched with their eukaryotic homologue and hypothesized cellular function. [1] The prokaryotic cytoskeleton is the collective name for all structural filaments in prokaryotes. [2] Some of these proteins are analogues of those in eukaryotes, while others are unique to prokaryotes.
Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils.It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.
Cytoskeletal proteins are usually correlated with cell shape, DNA segregation and cell division in prokaryotes and eukaryotes. Which proteins fulfill which task is very different. For example, DNA segregation in all eukaryotes happens through use of tubulin, but in prokaryotes either WACA proteins, actin-like or tubulin-like proteins can be used.
Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene. [5] Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types.
The prokaryotic cytoskeleton is less well-studied but is involved in the maintenance of cell shape, polarity and cytokinesis. [10] The subunit protein of microfilaments is a small, monomeric protein called actin. The subunit of microtubules is a dimeric molecule called tubulin. Intermediate filaments are heteropolymers whose subunits vary among ...
These are highly diverse, and contain homologues of the eukaryote proteins actin and tubulin. The cytoskeleton provides the capability for movement within the cell. [7] Most prokaryotes are between 1 and 10 μm, but they vary in size from 0.2 μm in Thermodiscus spp. and Mycoplasma genitalium to 750 μm in Thiomargarita namibiensis. [8] [9]
This allows for the length and flexibility of the actin binding protein to be decided. The actin-filament cross-links involve alpha-actinin, which is a functional anti-parallel dimer. [ 1 ] It consists of an actin binding domain (ABD) connected to four spectrin repeats forming the central rod through a flexible neck region.
Alpha-actinin-2 is a 103.8 kDa protein composed of 894 amino acids. [6] [7] Each molecule is rod-shaped (35 nm in length) and it homodimerizes in an anti-parallel fashion.. Each monomer has an N-terminal actin-binding region composed of two calponin homology domains, two C-terminal EF hand domains, and four tandem spectrin-like repeats form the rod domain in the central region of the molecule.