Evidence for pre-folding vein development in the Oligo-Miocene Asmari Formation in the Central Zagros Fold Belt, Iran

International audienceIn order to understand the interplay between vein development and folding in the carbonates of the Oligo-Miocene Asmari Formation (one of the main hydrocarbon reservoir rocks) in Iran, several anticlines have been investigated in the central part of the Zagros folded belt. Combining observations of relative chronology between veins based on calcite-filling phases and crosscutting/abutting relationships, as well as aerial/satellite image interpretation on several anticlines allowed proposing a tectonic model highlighting the widespread development of veins and other extensional micro/meso-structures in the Central Zagros folded belt. Our data suggest that most of the veins affecting the Asmari formation predated the main Miocene-Pliocene folding episode. An early regional vein set striking N50° marked the onset of collisional stress build-up in the region. Then, N150° and N20° trending vein sets were initiated in response to local extension caused by large-scale flexure/drape folds above N-S and N140° basement faults reactivated under the regional NE compression. At the onset and during Miocene-Pliocene folding of the sedimentary cover, the early formed veins were reactivated (reopened and/or sheared) while duplexes, low angle reverse faults and thrusts formed. Beyond regional implications, this study puts emphasis on the need of carefully considering regional/local vein development predating folding as well as influence of underlying basement faults in models of folded-fractured reservoirs in fold-thrust belts

An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations

Protein-protein interactions govern almost all cellular functions. These complex networks of stable and transient associations can be mapped by affinity purification mass spectrometry (AP-MS) and complementary proximity-based labeling methods such as BioID. To exploit the advantages of both strategies, we here design and optimize an integrated approach combining AP-MS and BioID in a single construct, which we term MAC-tag. We systematically apply the MAC-tag approach to 18 subcellular and 3 sub-organelle localization markers, generating a molecular context database, which can be used to define a protein's molecular location. In addition, we show that combining the AP-MS and BioID results makes it possible to obtain interaction distances within a protein complex. Taken together, our integrated strategy enables the comprehensive mapping of the physical and functional interactions of proteins, defining their molecular context and improving our understanding of the cellular interactome.Peer reviewe