Catalytic cycling of human mitochondrial Lon protease

The mitochondrial Lon protease homolog (LonP1) hexamer controls mitochondrial health by digesting proteins from the mitochondrial matrix that are damaged or must be removed. Understanding how it is regulated requires characterizing its mechanism. Here, we show how human LonP1 functions, based on eight different conformational states that we determined by cryo-EM with a resolution locally extending to 3.6 Å for the best ordered states. LonP1 has a poorly ordered N-terminal part with apparent threefold symmetry, which apparently binds substrate protein and feeds it into its AAA+ unfoldase core. This translocates the extended substrate protein into a proteolytic cavity, in which we report an additional, previously unidentified Thr-type proteolytic center. Threefold rocking movements of the flexible N-terminal assembly likely assist thermal unfolding of the substrate protein. Our data suggest LonP1 may function as a sixfold cyclical Brownian ratchet controlled by ATP hydrolysis.

Ruga mechanics of soft-orifice closure under external pressure

Here, we report the closure resistance of a soft-material bilayer orifice increases against external pressure, along with ruga-phase evolution, in contrast to the conventional predictions of the matrix-free cylindrical-shell buckling pressure. Experiments demonstrate that the generic soft-material orifice creases in a threefold symmetry at a limit-load pressure of p / μ ≈ 1.20, where μ is the shear modulus. Once the creasing initiates, the triple crease wings gradually grow as the pressure increases until the orifice completely closes at p / μ ≈ 3.0. By contrast, a stiff-surface bilayer orifice initially wrinkles with a multifold symmetry mode and subsequently develops ruga-phase evolution, progressively reducing the orifice cross-sectional area as pressure increases. The buckling-initiation mode is determined by the layer's thickness and stiffness, and the pressure by two types of the layer's instability modes—the surface-layer-wrinkling mode for a compliant and the ring-buckling mode for a stiff layer. The ring-buckling mode tends to set the twofold symmetry for the entire post-buckling closure process, while the high-frequency surface-layer-wrinkling mode evolves with successive symmetry breaking to a final closure configuration of two- or threefold symmetry. Finally, we found that the threefold symmetry mode for the entire closure process provides the orifice's strongest closure resistance, and human saphenous veins remarkably follow this threefold symmetry ruga evolution pathway.

Complete Quantum Information in the DNA Genetic Code

We find that the degeneracies and many peculiarities of the DNA genetic code may be described thanks to two closely related (fivefold symmetric) finite groups. The first group has signature G=Z5⋊H where H=Z2.S4≅2O is isomorphic to the binary octahedral group 2O and S4 is the symmetric group on four letters/bases. The second group has signature G=Z5⋊GL(2,3) and points out a threefold symmetry of base pairings. For those groups, the representations for the 22 conjugacy classes of G are in one-to-one correspondence with the multiplets encoding the proteinogenic amino acids. Additionally, most of the 22 characters of G attached to those representations are informationally complete. The biological meaning of these coincidences is discussed.

Complete Quantum Information in the DNA Genetic Code

We find that the degeneracies and many peculiarities of the DNA genetic code may be described thanks to two closely related (fivefold symmetric) finite groups. The first group has signature $G=\mathbb{Z}_5 \rtimes H$ where $H=\mathbb{Z}_2 . S_4\cong 2O$ is isomorphic to the binary octahedral group $2O$ and $S_4$ is the symmetric group on four letters/bases. The second group has signature $G=\mathbb{Z}_5 \rtimes GL(2,3)$ and points out a threefold symmetry of base pairings. For those groups, the representations for the $22$ conjugacy classes of $G$ are in one-to-one correspondence with the multiplets encoding the proteinogenic amino acids. Additionally, most of the $22$ characters of $G$ attached to those representations are informationally complete. The biological meaning of these coincidences is discussed.

Complete Quantum Information in the DNA Genetic Code

We find that the degeneracies and many peculiarities of the DNA genetic code may be described thanks to two closely related (fivefold symmetric) finite groups. The first group has signature $G=\mathbb{Z}_5 \rtimes H$ where $H=\mathbb{Z}_2 . S_4\cong 2O$ is isomorphic to the binary octahedral group $2O$ and $S_4$ is the symmetric group on four letters/bases. The second group has signature $G=\mathbb{Z}_5 \rtimes GL(2,3)$ and points out a threefold symmetry of base pairings. For those groups, the representations for the $22$ conjugacy classes of $G$ are in one-to-one correspondence with the multiplets encoding the proteinogenic amino acids. Additionally, most of the $22$ characters of $G$ attached to those representations are informationally complete. The biological meaning of these coincidences is discussed.