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A previously unknown mechanism relies on intrinsically inactive σ factor more

Bacteria pre-invest in motile behavior more

Density effects impair chemotactic behavior more

Everyone following Formula 1 knows that securing the pole position is not simple. The same is true for many proteins in rod-shaped bacteria like Myxococcus xanthus: they must localize to the cell poles to function properly. In a recent publication in Nature Microbiology, scientists from the Max Planck Institute for Terrestrial Microbiology together with scientists from the Technical University in Munich unraveled a novel mechanism for how a protein can reach pole position. more

Hydrogen gas is a green energy carrier. Microorganisms use dedicated enzymes called hydrogenases to convert this gas into energy. One of the model enzymes is [Fe]-hydrogenase (Hmd) that catalyzes the reversible hydride transfer between H₂ and the methanogenic C₁-carrier tetrahydromethanopterin using a unique prosthetic group, the FeGP cofactor. Up to now, Hmd, its paralogue (HmdII), and the FeGP cofactor were identified only in archaea. Scientists at the Max Planck Institute for Terrestrial Microbiology in Marburg and collaborators at the Max Plank Institute for Biophysics in Frankfurt and Freie Universität Berlin now discovered that bacteria are also able to produce HmdII and the FeGP cofactor, and showed that bacterial HmdII uses the bacterial C1-carrier, tetrahydrofolate. This finding has a great potential for biotechnological development of Hmd variants that function in bacteria. more