Compositional signatures of the Cenozoic sedimentary succesions of the Malaguide Complex (Betic Cordillera, Spain)

The studied Cenozoic sedimentary successions consist of deposits from continental/shallow-water to deep-marine environments of the Malaguide Complex (Betic Cordillera) outcropping in the Sierra Espuña area (SE Spain). The aim of this study is to characterize the composition, source area(s) provenance and weathering processes of these sedimentary successions from the pre-orogenic (Paleocene-Early Oligocene) to the syn-orogenic (Late Oligocene-Early Miocene) stage using petrological and geochemical methodologies. The studied sandstones are mainly quartzolithic with abundant metamorphic and sedimentary lithic fragments. In particular, the composition of samples from the pre-orogenic cycle is mainly carbonate with important siliciclastic components that occur within the medium to fine grained arenites. The composition of samples from the syn-orogenic cycle is characterized by a sharp change from carbonate to siliciclastic terms. Thus, the composition of the overall sandstone samples is very heterogeneous and suggests a source area mainly characterized by the Malaguide basement and lower units of the Internal Betic Zone, that partially compose the Mesomediterranean Microplate. The geochemical proxies suggest a provenance mainly from felsic source area with a minor supply from mafic rocks in some samples of the syn-orogenic stage. Furthermore, palaeoweathering indices indicate low to moderate weathering conditions for the sources. The Cenozoic sedimentary successions of the Malaguide Complex played an important role in the geodynamic evolution of the Betic Cordillera that represents the key tectonic element of the western domains of the Mesomediterranean Microplate.

Sub-Cellular Localization and Complex Formation by Aminoacyl-tRNA Synthetases in Cyanobacteria: Evidence for Interaction of Membrane-Anchored ValRS with ATP Synthase

tRNAs are charged with cognate amino acids by aminoacyl-tRNA synthetases (aaRSs) and subsequently delivered to the ribosome to be used as substrates for gene translation. Whether aminoacyl-tRNAs are channeled to the ribosome by transit within translational complexes that avoid their diffusion in the cytoplasm is a matter of intense investigation in organisms of the three domains of life. In the cyanobacterium Anabaena sp. PCC 7120, the valyl-tRNA synthetase (ValRS) is anchored to thylakoid membranes by means of the CAAD domain. We have investigated whether in this organism ValRS could act as a hub for the nucleation of a translational complex by attracting other aaRSs to the membranes. Out of the 20 aaRSs, only ValRS was found to localize in thylakoid membranes whereas the other enzymes occupied the soluble portion of the cytoplasm. To investigate the basis for this asymmetric distribution of aaRSs, a global search for proteins interacting with the 20 aaRSs was conducted. The interaction between ValRS and the FoF1 ATP synthase complex here reported is of utmost interest and suggests a functional link between elements of the gene translation and energy production machineries.