Calmodulin Triggers Activity-Dependent rRNA Biogenesis via Interaction with DDX21.

Protein synthesis in response to neuronal activity, known as activity-dependent translation, is critical for synaptic plasticity and memory formation. However, the signaling cascades that couple neuronal activity to the translational events remain elusive. In this study, we identified the role of calmodulin (CaM), a conserved Ca-binding protein, in ribosomal RNA (rRNA) biogenesis in neurons.

Superhydrophobic Coatings Prepared by the in Situ Growth of Silicone Nanofilaments on Alkali-Activated Geopolymers Surface.

As a highly hydrophobic and good environmental durable material, silicone nanofilaments have shown great advantages in the construction of superhydrophobic coatings. However, the synthesis of these materials has always been limited to the application of trifunctional organosilane monomers under the action of acidic catalysts. For the first time, long-chain polymeric hydrogenated siloxane-poly(methyl-hydrosiloxane) (PMHS) was used to synthesize rapidly silicone nanofilaments in situ under alkaline conditions.

Development of near-zero water consumption cement materials via the geopolymerization of tektites and its implication for lunar construction.

The environment on the lunar surface poses some difficult challenges to building long-term lunar bases; therefore, scientists and engineers have proposed the creation of habitats using lunar building materials. These materials must meet the following conditions: be resistant to severe lunar temperature cycles, be stable in a vacuum environment, have minimal water requirements, and be sourced from local Moon materials. Therefore, the preparation of lunar building materials that use lunar resources is preferred.

Structural studies of P-type ATPase-ligand complexes using an X-ray free-electron laser.

Membrane proteins are key players in biological systems, mediating signalling events and the specific transport of e.g. ions and metabolites.

Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA.

The 23S rRNA nucleotide m(2)G2445 is highly conserved in bacteria, and in Escherichia coli this modification is added by the enzyme YcbY. With lengths of around 700 amino acids, YcbY orthologs are the largest rRNA methyltransferases identified in Gram-negative bacteria, and they appear to be fusions from two separate proteins found in Gram-positives. The crystal structures described here show that both the N- and C-terminal halves of E.

Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans.

Argininosuccinate lyase (ASL) is an important enzyme in arginine synthesis and the urea cycle, which are highly conserved from bacteria to eukaryotes. The gene encoding Streptococcus mutans ASL (smASL) was amplified and cloned into expression vector pET28a. The recombinant smASL protein was expressed in a soluble form in Escherichia coli strain BL21 (DE3) and purified to homogeneity by two-step column chromatography.

Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m(2)G2445 methyltransferase RlmL from Escherichia coli.

The RlmL (YcbY) protein in Escherichia coli is an rRNA methyltransferase that is specific for m(2)G2445 modification of 23S RNA. The rlmL gene was cloned into the expression vector pET28a and expressed in the host E. coli strain BL21 (DE3).

Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation.

Dimeric effectors caspase 3 and caspase 7 are activated by initiator caspase processing. In this study, we report the crystal structures of effector caspase 6 (CASP6) zymogen and N-Acetyl-Val-Glu-Ile-Asp-al-inhibited CASP6. Both of these forms of CASP6 have a dimeric structure, and in CASP6 zymogen the intersubunit cleavage site (190)TEVD(193) is well structured and inserts into the active site.

Crystal structures of catalytic intermediates of human selenophosphate synthetase 1.

Selenophosphate synthetase catalyzes the synthesis of the highly active selenium donor molecule selenophosphate, a key intermediate in selenium metabolism. We have determined the high-resolution crystal structure of human selenophosphate synthetase 1 (hSPS1). An unexpected reaction intermediate, with a tightly bound phosphate and ADP at the active site has been captured in the structure.