Tracking Public Support for Japan\u27s Remilitarization Policies: An Examination of Elitist and Pluralist Governance

Has Japan’s post-Second World War transformation into one of the most militarily capable nations been the result of 60 years of truly representative government? This research compares government-collected opinion polls to policy trends and actions, to determine whether the case of Japan’s remilitarization argues for or against the country’s democratic quality. For the purpose of this research, the size of Japan’s military and its legislative freedom to act as a more conventional military were considered the most pertinent militarization policies. Results indicated that those policies were consistently unjustified by measured opinion, suggesting elitist policy formation. However, other policy areas, such as Japan’s military budget, participation in UN peacekeeping, and national defense capability, have indicated a more pluralist model of policy formation. Therefore, results suggest that the country’s remilitarization has been the product of both elitist and pluralist governance

Synthesis of GNAT PA3944 Substrate Analogs

The Gcn5-related N-acetyltransferase (GNAT) superfamily is responsible for diverse biological functions and is critically important in cellular and metabolic processes in all kingdoms of life. GNATs transfer an acetyl-group from an active donor, typically acetyl-coenzyme A (AcCoA), to a primary amine of an acceptor substrate. Members of this family are well known for their roles in aminoglycoside antibiotic resistance, histone modification, protein acetylation, xenobiotic metabolism, and other cellular processes.1, 2 A small subset of bacterial GNAT enzymes have been studied and characterized both structurally and functionally, but the function of the vast majority remains unknown. Most of the reported 3D crystallographic structures of GNATs contain no acceptor substrate bound in their active sites. We previously screened the PA3944 protein against a panel of potential substrates and found the enzyme exhibited the highest activity toward aspartame, polymyxin B and colistin (polymyxin E).3 Our project involves the synthesis of molecular analogs of previously identified functionally relevant acceptor substrates that will be co-crystallized with GNAT-PA3944, in particular simplified derivatives of polymyxin B including NANMO and AAB, and we have shown that NANMO is as efficient as polymyxin B as a substrate. The ligand-bound crystallographic structures will provide insight into the structural features of the active site that are involved in substrate recognition and advance our understanding of types of substrates recognized by this enzyme of unknown function. Syntheses of NANMO and AAB will be described, along with modeling and substrate efficiency