The role of the perovskite lattice oxygen in the oxygen evolution reaction (OER) is systematically studied in the PrBaCo2O5+δ family. The reduced number of physical/chemical variables combined with in‐depth characterizations such as neutron dif‐fraction, O K‐edge X‐ray absorption spectroscopy (XAS), electron energy loss spectroscopy (EELS), magnetization and scanning transmission electron microscopy (STEM) studies, helps investigating the complex correlation between OER activity and a single perovskite property, such as the oxygen content. Larger amount of oxygen vacancies appears to facilitate the OER, possibly contributing to the mechanism involving the oxidation of lattice oxygen, i.e., the lattice oxygen evolution reaction (LOER). Furthermore, not only the number of vacancies but also their local arrangement in the perovskite lattice influences the OER activity, with a clear drop for the more stable, ordered stoichiometry.
NDK5 promotes assembly of motile cilia and flagella with its structure and protein phosphorylation–related reactions instead of the canonical NDK activity. The novel mechanisms and dominant-negative effect of mutated functional NDK5 reveal the remarkable versatility of a molecular platform that is used in diverse cellular processes.
The radial spoke is a key element in a transducer apparatus controlling the motility of eukaryotic cilia. The transduction biomechanics is a long-standing question in cilia biology. The radial spoke has three regions – a spoke head, a bifurcated neck and a stalk. While the neck and the stalk are asymmetric, two-fold symmetry of the head has remained controversial. In this work we used single particle cryo-EM analysis to generate 3D structure of the whole radial spoke at unprecedented resolution. We show the head region at 15Å resolution and confirm two-fold symmetry. Using distance constraints generated by crosslinking mass spectrometry we locate two components, RSP2 and 4 at the head/neck regions. Our biophysical analysis of isolated RSPs 4, 9, and 10 affirmed their oligomeric state. Our results enabled us to redefine the boundaries of the regions and propose a model of organization of the radial spoke component proteins.
HSP40s are regarded as cochaperones, perpetually shuttling client polypeptides to HSP70s for refolding. However, many HSP40s that are central for disparate processes diverge from this paradigm. To elucidate the noncanonical mechanisms, we investigated HSP40 in the radial spoke (RS) complex in flagella. Disruption of the gene by the MRC1 transposon in Chlamydomonas resulted in jerky flagella. Traditional electron microscopy, cryo-electron tomography, and sub-tomogram analysis revealed RSs of various altered morphologies that, unexpectedly, differed between the two RS species. This indicates that HSP40 locks the RS into a functionally rigid conformation, facilitating its interactions with the adjacent central pair apparatus for transducing locally varied mechanical feedback, which permits rhythmic beating. Missing HSP40, like missing RSs, could be restored in a tip-to-base direction when HSP40 mutants fused with a HSP40 donor cell. However, without concomitant de novo RS assembly, the repair was exceedingly slow, suggesting HSP40/RS-coupled intraflagellar trafficking and assembly. Biochemical analysis and modeling uncovered spoke HSP40’s cochaperone traits. On the basis of our data, we propose that HSP40 accompanies its client RS precursor when traveling to the flagellar tip. Upon arrival, both refold in concert to assemble into the mature configuration. HSP40’s roles in chaperoning and structural maintenance shed new light on its versatility and flagellar biology.
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