Amongst other threats, the world's oceans are faced with man-made pollution, including an increasing number of microparticulate pollutants. Sponges, aquatic filter-feeding animals, are able to incorporate fine foreign particles, and thus may be a potential bioindicator for microparticulate pollutants. To address this question, 15 coral reef demosponges sampled around Bangka Island (North Sulawesi, Indonesia) were analyzed for the nature of their foreign particle content using traditional histological methods, advanced light microscopy, and Raman spectroscopy. Sampled sponges accumulated and embedded the very fine sediment fraction (< 200 µm), absent in the surrounding sand, in the ectosome (outer epithelia) and spongin fibers (skeletal elements), which was confirmed by two-photon microscopy. A total of 34 different particle types were identified, of which degraded man-made products, i.e., polystyrene, cotton, titanium dioxide and blue-pigmented particles, were incorporated by eight specimens at concentrations between 91 to 612 particle/g dry sponge tissue. As sponges can weigh several hundreds of grams, we conservatively extrapolate that sponges can incorporate on average 10,000 microparticulate pollutants in their tissue. The uptake of particles, however, appears independent of the material, which suggests that the fluctuation in material ratios is due to the spatial variation of surrounding microparticles. Therefore, sponges have a strong potential to biomonitor microparticulate pollutants, such as microplastics and other degraded industrial products.

SummaryProteasomes are self-compartmentalizing proteases that function at the core of the cellular protein degradation machinery in eukaryotes, archaea, and some bacteria. Although their evolutionary history is under debate, it is thought to be linked to that of the bacterial protease HslV and the hypothetical bacterial protease Anbu (ancestral beta subunit). Here, together with an extensive bioinformatic analysis, we present the first biophysical characterization of Anbu. Anbu forms a dodecameric complex with a unique architecture that was only accessible through the combination of X-ray crystallography and small-angle X-ray scattering. While forming continuous helices in crystals and electron microscopy preparations, refinement of sections from the crystal structure against the scattering data revealed a helical open-ring structure in solution, contrasting the ring-shaped structures of proteasome and HslV. Based on this primordial architecture and exhaustive sequence comparisons, we propose that Anbu represents an ancestral precursor at the origin of self-compartmentalization.

over, they are often invasive, [2] require high vacuum, [3] or preclude real-space information, [4] thus preventing in situ studies of materials. These two characterization levels are also reflected in current research efforts, for instance, on metalorganic frameworks (MOFs) that mainly focus on two distinct aspects: molecular structures being tuned and bulk properties being measured. [5] MOF chemists often vary the molecular building units (e.g., installation of a functional group) and examine the corresponding change in the performance of a bulk sample (e.g., gas adsorption isotherm). Alteration of MOF particle properties can be caused twofold: (1) by differences in "extrinsic properties", that is, physical parameters like their particle size, shape, and surface structure, or (2) by variations in "intrinsic properties" ruled by chemical attributes of the framework. These include casual differences in the composition of building blocks, [6] crystallinity, [7] functionalization, [8] and defects, [2] but also designed variations as in multivariate MOFs. The interplay of both kinds of properties determines the overall performance for any application; the mutual impact of intrinsic and extrinsic variations correlated to any change in individual particle properties in situ is challenging to explore in a correlative manner.At present, an enormous characterization gap exists between the study of the crystal structure of a material and its bulk properties. Individual particles falling within this gap cannot be fully characterized in a correlative manner by current methods. The authors address this problem by exploiting the noninvasive nature of optical microscopy and spectroscopy for the correlative analysis of metal-organic framework particles in situ. They probe the intrinsic as well as extrinsic properties in a correlated manner. The authors show that the crystal shape of MIL-88A strongly impacts its optical absorption. Furthermore, the question of how homogeneously water is distributed and adsorbed within one of the most promising materials for harvesting water from humid air, MOF-801, is addressed. The results demonstrate the considerable importance of the particle level and how it can affect the property of the material.

While protein ubiquitination was long believed to be a truly eukaryotic feature, recently sequenced genomes revealed complete ubiquitin (Ub) modification operons in archaea. Here, we present the structural and mechanistic characterization of an archaeal Rpn11 deubiquitinase from Caldiarchaeum subterraneum, CsRpn11, and its role in the processing of CsUb precursor and ubiquitinated proteins. CsRpn11 activity is affected by the catalytic metal ion type, small molecule inhibitors, sequence characteristics at the cleavage site, and the folding state of CsUb-conjugated proteins. Comparison of CsRpn11 and CsRpn11–CsUb crystal structures reveals a crucial conformational switch in the CsRpn11 Ins-1 site, which positions CsUb for catalysis. The presence of this transition in a primordial soluble Rpn11 thus predates the evolution of eukaryotic Rpn11 immobilized in the proteasomal lid. Complementing phylogenetic studies, which designate CsRpn11 and CsUb as close homologs of the respective eukaryotic proteins, our results provide experimental support for an archaeal origin of protein ubiquitination.