No abstract

Hydrogen bond-mediated self-assembly is a powerful strategy for generating large structures from smaller subunits. The synthesis of molecules containing two isophthalic acid units covalently attached to a rigid aromatic spacer is described. By normal pairing of carboxylic acids into hydrogen-bonded dimers, these molecules self-assemble in organic solvents to form either a series of linear aggregates or a cyclic hexamer. These molecules were linked to the core of a family of polyether dendrimers, which caused the hexamer to be formed preferentially. The stability of the hexamer depended on the generation number of the dendrimer. The largest of these hydrogen-bonded macromolecular assemblies is roughly disk-shaped with a 9-nanometer diameter and a 2-nanometer thickness. Its size and molecular mass (34,000 daltons) are comparable to that of small proteins.

Human RNA-binding protein (HuR), a ubiquitously expressed member of the Hu protein family, plays an important role in mRNA degradation and has been implicated as a key post-transcriptional regulator. HuR contains three RNA-recognition motif (RRM) domains. The two N-terminal tandem RRM domains can selectively bind AU-rich elements (AREs), while the third RRM domain (RRM3) contributes to interactions with the poly-A tail of target mRNA and other ligands. Here, the X-ray structure of two methylated tandem RRM domains (RRM1/2) of HuR in their RNA-free form was solved at 2.9 Å resolution. The crystal structure of RRM1/2 complexed with target mRNA was also solved at 2.0 Å resolution; comparisons of the two structures show that HuR RRM1/2 undergoes conformational changes upon RNA binding. Fluorescence polarization assays (FPA) were used to study the protein-RNA interactions. Both the structure and the FPA analysis indicated that RRM1 is the primary ARE-binding domain in HuR and that the conformational changes induce subsequent contacts of the RNA substrate with the inter-domain linker and RRM2 which greatly improve the RNA-binding affinity of HuR.

Understanding marine environmental change and associated biological turnover across the Palaeocene–Eocene Thermal Maximum (PETM; ~56 Ma)—the most pronounced Cenozoic short-term global warming event—is important because of the potential role of the ocean in atmospheric CO2 drawdown, yet proxies for tracing marine productivity and oxygenation across the PETM are limited and results remain controversial. Here we show that a high-resolution record of South Atlantic Ocean bottom water oxygenation can be extracted from exceptionally preserved magnetofossils—the bioinorganic magnetite nanocrystals produced by magnetotactic bacteria (MTB) using a new multiscale environmental magnetic approach. Our results suggest that a transient MTB bloom occurred due to increased nutrient supply. Bottom water oxygenation decreased gradually from the onset to the peak PETM. These observations provide a record of microbial response to the PETM and establish the value of magnetofossils as palaeoenvironmental indicators.