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Abstract YidC/Alb3/Oxa1 family proteins are involved in the insertion and assembly of membrane proteins. The core five transmembrane regions of YidC, which are conserved in the protein family, form a positively charged cavity open to the cytoplasmic side. The cavity plays an important role in membrane protein insertion. In all reported structural studies of YidC, the second cytoplasmic loop (C2 loop) was disordered, limiting the understanding of its role. Here, we determined the crystal structure of YidC including the C2 loop at 2.8 Å resolution with R / R free = 21.8/27.5. This structure and subsequent molecular dynamics simulation indicated that the intrinsic flexible C2 loop covered the positively charged cavity. This crystal structure provides the coordinates of the complete core region including the C2 loop, which is valuable for further analyses of YidC. [ABSTRACT FROM AUTHOR]

Abstract: A new sledge net system using propulsion vehicles has been developed to sample more efficiently the demersal juveniles of marine organisms. A net attached to a sledge maneuvered by a SCUBA diver who uses operating switches on a steering handle to adjust the altitude of the sledge and the position of the tickler chains to ensure that the footcloth of the mouth of the net remains in constant contact with the bottom surface. Video camera, flow meter, compass, and dive computers are positioned on the sledge net in the view of the diver. Given that the system can attain speeds of 70cms−1, the net can be employed to capture highly mobile fish. Unlike most boat-based net sampling methods, the use of propulsion vehicles means that there are no sound or vibration disturbances due to the boat and tow ropes typically used to maneuver these types of sampling nets. Marine fauna was collected at monthly intervals over a two-year period in a sampling area along the southern coast of Hokkaido, Japan. A total of 2641 specimens comprising 61 species and including five species which were the first records for the region were collected. These findings suggest that the new sledge net system employing propulsion vehicles was effective for sampling demersal juveniles, particularly in situations where sledge nets towed by boats or push nets cannot be deployed. [Copyright &y& Elsevier]

Abstract The β-barrel assembly machinery (BAM) complex mediates the assembly of β-barrel membrane proteins in the outer membrane. BepA, formerly known as YfgC, interacts with the BAM complex and functions as a protease/chaperone for the enhancement of the assembly and/or degradation of β-barrel membrane proteins. To elucidate the molecular mechanism underlying the dual functions of BepA, its full-length three-dimensional structure is needed. Here, we report the crystal structure of full-length BepA at 2.6-Å resolution. BepA possesses an N-terminal protease domain and a C-terminal tetratricopeptide repeat domain, which interact with each other. Domain cross-linking by structure-guided introduction of disulfide bonds did not affect the activities of BepA in vivo , suggesting that the function of this protein does not involve domain rearrangement. The full-length BepA structure is compatible with the previously proposed docking model of BAM complex and tetratricopeptide repeat domain of BepA. Graphical Abstract Unlabelled Image Highlights • Crystal structure (2.6 Å) of full-length BepA, β-barrel assembly-enhancing protease BepA • Crystal structure represents both its functional and resting states. • Functional model of BepA was proposed. [ABSTRACT FROM AUTHOR]