Engineering geological map of the Chiavari city area (Liguria, Italy)

An engineering geological map at a scale of 1:10,000 of the Chiavari city area (Northern Italy) – a major tourist and economic attraction of the Ligurian East Riviera – is presented in this paper. The municipality land shows an excellent geomorphological case-study of the well-known Ligurian coast: a floodplain, fairly wide and inhabited, formed by several floods of the two main rivers, a hill hinterland, reasonably inhabited, developed in marly limestones and sandy shales flysch and the coast – featuring cliffs and narrow pebbly beaches – deeply modified. This map was compiled by combining available geological data with a new engineering geomorphological field survey and including geotechnical data which were obtained from studies carried out for town planning and building purposes. On the basis of the critical review of the available lithostratigraphic data from drilling, as well as geotechnical and geophysical analyses carried out between 1981 and 2010 on the municipality land, an engineering geologica..

ARL2 and BART Enter Mitochondria and Bind the Adenine Nucleotide Transporter

The ADP-ribosylation factor-like 2 (ARL2) GTPase and its binding partner binder of ARL2 (BART) are ubiquitously expressed in rodent and human tissues and are most abundant in brain. Both ARL2 and BART are predominantly cytosolic, but a pool of each was found associated with mitochondria in a protease-resistant form. ARL2 was found to lack covalent N-myristoylation, present on all other members of the ARF family, thereby preserving the N-terminal amphipathic α-helix as a potential mitochondrial import sequence. An overlay assay was developed to identify binding partners for the BART·ARL2·GTP complex and revealed a specific interaction with a protein in bovine brain mitochondria. Purification and partial microsequencing identified the protein as an adenine nucleotide transporter (ANT). The overlay assay was performed on mitochondria isolated from five different tissues from either wild-type or transgenic mice deleted for ANT1. Results confirmed that ANT1 is the predominant binding partner for the BART·ARL2·GTP complex and that the structurally homologous ANT2 protein does not bind the complex. Cardiac and skeletal muscle mitochondria from ant1(−)/ant1(−) mice had increased levels of ARL2, relative to that seen in mitochondria from wild-type animals. We conclude that the amount of ARL2 in mitochondria is subject to regulation via an ANT1-sensitive pathway in muscle tissues