A team of Japanese researchers led by Homma’s laboratory of Nagoya University have now purified the stator protein MotA from a bacterium found in hot springs (Aquifex aeolicus) and analyzed its three-dimensional structure using electron microscopy mainly in cooperation with Namba’s laboratory of Osaka University. They found that it can form a structure of four MotA molecules (called a tetramer), which differs in shape from the previously predicted complex. The study was recently published in Scientific Reports.
The MotA protein spans the bacterial membrane, and has previously been shown to form a tetramer complex with another transmembrane protein, MotB, creating the stator. In this latest work, MotA was expressed and purified from A. aeolicus, and found to be structurally stable. Assessment of its interactive potential revealed it can form a tetramer even in the absence of MotB. More. Paper. (public access) – Norihiro Takekawa, Naoya Terahara, Takayuki Kato, Mizuki Gohara, Kouta Mayanagi, Atsushi Hijikata, Yasuhiro Onoue, Seiji Kojima, Tsuyoshi Shirai, Keiichi Namba, Michio Homma. The tetrameric MotA complex as the core of the flagellar motor stator from hyperthermophilic bacterium. Scientific Reports, 2016; 6: 31526 DOI: 10.1038/srep31526
Often pointed to by ID theorists as an example of design in nature.
See also: “Incredible ”bacterial rotors , varying torques, imaged
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