Parameterized Modeling and Calibration for Orbital Error in TanDEM-X Bistatic SAR Interferometry over Complex Terrain Areas

The TerraSAR-X add-on for Digital Elevation Measurements (TanDEM-X) bistatic system provides high-resolution and high-quality interferometric data for global topographic measurement. Since the twin TanDEM-X satellites fly in a close helix formation, they can acquire approximately simultaneous synthetic aperture radar (SAR) images, so that temporal decorrelation and atmospheric delay can be ignored. Consequently, the orbital error becomes the most significant error limiting high-resolution SAR interferometry (InSAR) applications, such as the high-precision digital elevation model (DEM) reconstruction, subway and highway deformation monitoring, landslide monitoring and sub-canopy topography inversion. For rugged mountainous areas, in particular, it is difficult to estimate and correct the orbital phase error in TanDEM-X bistatic InSAR. Based on the rigorous InSAR geometric relationship, the orbital phase error can be attributed to the baseline errors (BEs) after fixing the positions of the master SAR sensor and the targets on the ground surface. For the constraint of the targets at a study scene, the freely released TanDEM-X DEM can be used, due to its consistency with the TanDEM-X bistatic InSAR-measured height. As a result, a parameterized model for the orbital phase error estimation is proposed in this paper. In high-resolution and high-precision TanDEM-X bistatic InSAR processing, due to the limited precision of the navigation systems and the uneven baseline changes caused by the helix formation, the BEs are time-varying in most cases. The parameterized model is thus built and estimated along each range line. To validate the proposed method, two mountainous test sites located in China (i.e., Fuping in Shanxi province and Hetang in Hunan province) were selected. The obtained results show that the orbital phase errors of the bistatic interferograms over the two test sites are well estimated. Compared with the widely applied polynomial model, the residual phase corrected by the proposed method contains little undesirable topography-dependent phase error, and avoids unexpected height errors ranging about from −6 m to 3 m for the Fuping test site and from −10 m to 8 m for the Hetang test site. Furthermore, some fine details, such as ridges and valleys, can be clearly identified after the correction. In addition, the two components of the orbital phase error, i.e., the residual flat-earth phase error and the topographic phase error caused by orbital error, are separated and quantified based on the parameterized expression. These demonstrate that the proposed method can be used to accurately estimate and mitigate the orbital phase error in TanDEM-X bistatic InSAR data, which increases the feasibility of reconstructing high-resolution and high-precision DEM. The rigorous geometric constraint, the refinement of the initial baseline parameters, and the assessment for height errors based on the estimated BEs are investigated in the discussion section of this paper.

A Model for DHX15 Mediated Disassembly of A-Complex Spliceosomes

A critical step of pre-mRNA splicing is the recruitment of U2 snRNP to the branch point sequence of an intron. U2 snRNP conformation changes extensively during branch helix formation and several RNA-dependent-ATPases are implicated in the process. However, the molecular mechanisms involved remain to be fully dissected. We took advantage of the differential nucleotide triphosphates requirements for DExD/H-box enzymes to probe their contributions to in vitro spliceosome assembly. Both ATP and GTP hydrolysis support the formation of A-complex, indicating the activity of a DEAH-enzyme because DEAD-enzymes are selective for ATP. We immunodepleted DHX15 to assess its involvement and although splicing efficiency decreases with reduced DHX15, A-complex accumulation incongruently increases. DHX15 depletion also results in the persistence of the atypical ATP-independent interaction between U2 snRNP and a minimal substrate that is otherwise destabilized in the presence of either ATP or GTP. These results lead us to hypothesize that DHX15 plays a quality control function in U2 snRNP's engagement with an intron. In efforts to identify the RNA target of DHX15, we determined that an extended polypyrimidine tract is not necessary for disruption of the atypical interaction between U2 snRNP and the minimal substrate. We also examined U2 snRNA by RNase H digestion and identified nucleotides in the branch binding region that become accessible with both ATP and GTP hydrolysis, again implicating a DEAH-enzyme. Together, our results demonstrate that multiple ATP-dependent rearrangements are likely involved in U2 snRNP addition to the spliceosome and that DHX15 can have an expanded role in splicing.

Structural insights into the gating mechanism of human Cx43/GJA1 gap junction channel

Connexin family proteins assemble into hexameric hemichannels in a cell membrane, which dock together between two adjacent membranes to form gap junction intercellular channels (GJIChs). The most ubiquitously expressed connexin Cx43 plays important roles in numerous biological processes. Here we report cryo-EM structures of Cx43 GJIChs at 3.1–3.6 Å resolutions, which show dynamic conformational changes of N-terminal helices (NTHs) caused by pH change or C-terminal truncation. Cx43 GJIChs in a channel-closing condition contain 12 protomers in gate-covering NTH (GCN) conformation, while those in opening conditions have varying compositions of GCNs and pore-lining NTHs (PLNs) resulting in various pore dimensions and electrostatic surface potentials. GCN-to-PLN transition accompanies π-helix formation in the first transmembrane helix (TM1), movement of TM2-4 that creates a side opening to the membrane, and structural stabilization of the cytoplasmic loop. Our study provides structural insights into the intercellular ion/metabolite transfer and the lateral lipid transport through Cx43 GJICh.

Phototunable self-oscillating system driven by a self-winding fiber actuator

Self-oscillating systems that enable autonomous, continuous motions driven by an unchanging, constant stimulus would have significant applications in intelligent machines, advanced robotics, and biomedical devices. Despite efforts to gain self-oscillations have been made through artificial systems using responsive soft materials of gels or liquid crystal polymers, these systems are plagued with problems that restrict their practical applicability: few available oscillation modes due to limited degrees of freedom, inability to control the evolution between different modes, and failure under loading. Here we create a phototunable self-oscillating system that possesses a broad range of oscillation modes, controllable evolution between diverse modes, and loading capability. This self-oscillating system is driven by a photoactive self-winding fiber actuator designed and prepared through a twistless strategy inspired by the helix formation of plant-tendrils, which endows the system with high degrees of freedom. It enables not only controllable generation of three basic self-oscillations but also production of diverse complex oscillatory motions. Moreover, it can work continuously over 1270000 cycles without obvious fatigue, exhibiting high robustness. We envision that this system with controllable self-oscillations, loading capability, and mechanical robustness will be useful in autonomous, self-sustained machines and devices with the core feature of photo-mechanical transduction.

Folding of VemP into translation-arresting secondary structure is driven by the ribosome exit tunnel

The ribosome is a fundamental biomolecular complex responsible for protein production in cells. Nascent proteins emerge from the ribosome through a tunnel, where they may interact with the tunnel walls or small molecules such as antibiotics. These interactions can cause translational arrest with notable physiologic consequences. Here, we studied the arrest caused by the regulatory peptide VemP, which is known to form an α-helix in the ribosome tunnel near the peptidyl transferase center under specific conditions. We used all-atom molecular dynamics simulations of the entire ribosome and circular dichroism spectroscopy to study the driving forces of helix formation and how VemP causes the translational arrest. To that aim, we compared VemP dynamics in the ribosome tunnel with its dynamics in solution. We show that the VemP sequence has a low helical propensity in water and that the propensity is higher in more hydrophobic solvents. We propose that helix formation within the ribosome is driven by the tunnel environment and that a portion of VemP acts as an anchor. This anchor might slow down VemP progression through the tunnel enabling the α-helix formation, which causes the elongation arrest.