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microtubule : ウィキペディア英語版
microtubule

Microtubules (''micro-'' + ''tube'' + ''-ule'') are a component of the cytoskeleton, found throughout the cytoplasm. These tubular polymers of tubulin can grow as long as 50 micrometres and are highly dynamic. The outer diameter of a microtubule is about 24 nm while the inner diameter is about 12 nm. They are found in eukaryotic cells, as well as some Bacteria, and are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin.〔https://www.rpi.edu/dept/bcbp/molbiochem/MBWeb/mb2/part1/microtub.htm〕
Microtubules are very important in a number of cellular processes. They are involved in maintaining the structure of the cell and, together with microfilaments and intermediate filaments, they form the cytoskeleton. They also make up the internal structure of cilia and flagella.They provide platforms for intracellular transport and are involved in a variety of cellular processes, including the movement of secretory vesicles, organelles, and intracellular macromolecular assemblies (see entries for dynein and kinesin). They are also involved in chromosome separation (mitosis and meiosis), and are the major constituents of mitotic spindles, which are used to pull apart eukaryotic chromosomes.
Microtubules are nucleated and organized by microtubule organizing centers (MTOCs), such as the centrosome found in the center of many animal cells or the basal bodies found in cilia and flagella, or the spindle pole bodies found in fungi.
There are many proteins that bind to microtubules, including the motor proteins kinesin and dynein, severing proteins like katanin, and other proteins important for regulating microtubule dynamics.
==Structure==

In Eukaryotes, microtubules are long, hollow cylinders made up of polymerised α- and β-tubulin dimers. The α and β-tubulin subunits are approximately 50% identical at the amino acid level, and each have a molecular weight of approximately 50 kDa.
These α/β-tubulin dimers polymerize end-to-end into linear protofilaments that associate laterally to form a single microtubule, which can then be extended by the addition of more α/β-tubulin dimers. Typically, microtubules are formed by the parallel association of thirteen protofilaments, although microtubules composed of fewer or more protofilaments have been observed ''in vitro''.〔Chrétien D, Metoz F, Verde F, Karsenti E, Wade RH. (Lattice defects in microtubules: protofilament numbers vary within individual microtubules ) J Cell Biol. 1992 Jun;117(5):1031-40.〕
Microtubules have a distinct polarity that is critical for their biological function. Tubulin polymerizes end to end, with the β-subunits of one tubulin dimer contacting the α-subunits of the next dimer. Therefore, in a protofilament, one end will have the α-subunits exposed while the other end will have the β-subunits exposed. These ends are designated the (−) and (+) ends, respectively. The protofilaments bundle parallel to one another with the same polarity, so, in a microtubule, there is one end, the (+) end, with only β-subunits exposed, while the other end, the (−) end, has only α-subunits exposed. While microtubule elongation can occur at both the (+) and (-) ends, it is significantly more rapid at the (+) end.
The lateral association of the protofilaments generates a pseudo-helical structure, with one turn of the helix containing 13 tubulin dimers, each from a different protofilament. There are two distinct types of interactions that can occur between the subunits of lateral protofilaments within the microtubule called the A-type and B-type lattices. In the A-type lattice, the lateral associations of protofilaments occur between adjacent α and β-tubulin subunits (i.e. an α-tubulin subunit from one protofilament interacts with a β-tubulin subunit from an adjacent protofilament). In the B-type lattice, the α and β-tubulin subunits from one protofilament interact with the α and β-tubulin subunits from an adjacent protofilament, respectively. Experimental studies have shown that the B-type lattice is the primary arrangement within microtubules. However, in most microtubules there is a seam in which tubulin subunits interact α-β.
Some species of ''Prosthecobacter'' also contain microtubules. The structure of these bacterial microtubules is similar to that of eukaryotic microtubules, consisting of a hollow tube of protofilaments assembled from heterodimers of bacterial tubulin A (BtubA) and bacterial tubulin B (BtubB). Both BtubA and BtubB share features of both α- and β-tubulin. Unlike eukaryotic microtubules, bacterial microtubules do not require chaperones to fold. In contrast to the 13 protofilaments of eukaryotic microtubules, bacterial microtubules comprise only five.〔

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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