The long-term and non-exclusive Auto-Parts Transaction in the Grerman Automotive Industry: A historical Comparision with the Japanese and US Supplier System (2)

本稿は、広島大学大学院社会科学研究科社会経済システム専攻、修士論文（張家華「自動車産業における部品取引の日独米比較―なぜドイツの部品取引は長期的かつ非専属的なのか―」（令和元年3 月）にもとづき、論旨と構成を維持したうえで、森良次が内容の大幅な修正、加筆（史実の充実、論点の追加、考察）を行っている

The long-term and non-exclusive Auto-Parts Transaction in the Grerman Automotive Industry: A historical Comparision with the Japanese and US Supplier System

本稿は、広島大学大学院社会科学研究科社会経済システム専攻、修士論文（張家華「自動車産業における部品取引の日独米比較―なぜドイツの部品取引は長期的かつ非専属的なのか―」（令和元年3月）を加筆・修正したものである

Masaru MARUYAMA's Italian Economic History and Post-Mass Production System

本稿は，丸山優（日本福祉大学名誉教授，2022 年 1 月 6 日逝去）のイタリア経済史および大量生産体制の歴史的オルタナティブに関する研究の解題を試みる． 　本稿では，①丸山の学問形成期の時代的・学術的背景と資本主義発展段階論の特徴を示したうえで，②イタリア経済史研究（南部農業史，ファシズムの経済政策）の要点・到達点を確認している．③また丸山が研究領域をイタリア経済史から大量生産体制の歴史的オルタナティブをめぐる問題へと拡大していった学術的背景・動向を跡づけている．解題departmental bulletin pape

Inner membrane YfgM–PpiD heterodimer acts as a functional unit that associates with the SecY/E/G translocon and promotes protein translocation

PpiD and YfgM are inner membrane proteins that are both composed of an N-terminal transmembrane segment and a C-terminal periplasmic domain. Escherichia coli YfgM and PpiD form a stable complex that interacts with the SecY/E/G (Sec) translocon, a channel that allows protein translocation across the cytoplasmic membrane. Although PpiD is known to function in protein translocation, the functional significance of PpiD-YfgM complex formation as well as the molecular mechanisms of PpiD-YfgM and PpiD/YfgM- Sec translocon interactions remain unclear. Here, we conducted genetic and biochemical studies using yfgM and ppiD mutants and demonstrated that a lack of YfgM caused partial PpiD degradation at its C-terminal region and hindered the membrane translocation of VemP, a Vibrio secretory protein in both Escherichia coli and Vibrio alginolyticus. While ppiD disruption also impaired VemP translocation, we found that the yfgM and ppiD double deletion exhibited no additive or synergistic effects. Together, these results strongly suggest that both PpiD and YfgM are required for efficient VemP translocation. Furthermore, our site-directed in vivo photo-crosslinking analysis revealed that the tetratricopeptide repeat domain of YfgM and a conserved structural domain (NC domain) in PpiD interact with each other and that YfgM, like PpiD, directly interacts with the SecG translocon subunit. Crosslinking analysis also suggested that PpiD/YfgM complex formation is required for these proteins to interact with SecG. In summary, we propose that PpiD and YfgM form a functional unit that stimulates protein translocation by facilitating proper interactions with the Sec translocon