Magnetization switching by the interaction between spins and charges has greatly brightened the future of spintronic memories. [1][2][3][4][5][6] This has been evident in the rapid development of spin transfer torque-magnetic random-access memory (STT-MRAM) as a mainstream non-volatile memory technology, in which a spin-polarized current is injected into magnetic tunnel junctions (MTJs) for cell programming. 7-18 However, as cell areas scale down to meet density and power demands, conventional STT-MRAM suffers from serious endurance and reliability issues due to the aging of the ultrathin MgO barrier and read disturbance. The challenge of lowering STT switching current densities to further reduce power consumption is still yet to be met. [19][20][21] The discovery of spin-orbit torque (SOT) switching in heavy metal/ferromagnetic metal/oxide heterostructures by applying an in-plane charge current to three-terminal devices provides a promising alternative mechanism. 22-28 It shows the potential to enhance the endurance and reliability of MRAM, while improving speed and reducing power consumption. [29][30][31][32] Thus, considerable research has been triggered to further elucidate the mechanism of SOT switching, which is currently described as magnetic reversal via two vector components, the damping-like (DL) and field-like (FL) torques. 33,34 Since the demonstration of perpendicular-anisotropy MgO/CoFeB MTJs (p-MTJs), the switching of perpendicular magnetization by SOT has become of particular interest. [33][34][35][36][37][38] However, an external magnetic field collinear with the charge current is required to execute deterministic switching of p-MTJs. This intrinsic constraint, combined with the three-terminal device configuration, is limiting the practical application of SOT-MRAM. [26][27][28]35 Great efforts have been made to eliminate the need
The solventogenic bacterium Clostridium acetobutylicum is an important species of the Clostridium community. To develop a fundamental tool that is useful for biological studies of C. acetobutylicum, we established a high resolution proteome reference map for this species. We identified 1206 spots representing 564 different proteins by mass spectrometry, covering approximately 50% of major metabolic pathways. To better understand the relationship between butanol tolerance and butanol yield, we performed a comparative proteomic analysis between the wild type strain DSM 1731 and the mutant Rh8, which has higher butanol tolerance and higher butanol yield. Comparative proteomic analysis of two strains at acidogenic and solventogenic phases revealed 102 differentially expressed proteins that are mainly involved in protein folding, solvent formation, amino acid metabolism, protein synthesis, nucleotide metabolism, transport, and others. Hierarchical clustering analysis revealed that over 70% of the 102 differentially expressed proteins in mutant Rh8 were either upregulated (e.g., chaperones and solvent formation related) or downregulated (e.g., amino acid metabolism and protein synthesis related) in both acidogenic and solventogenic phase, which, respectively, are only upregulated or downregulated in solventogenic phase in the wild type strain. This suggests that Rh8 cells have evolved a mechanism to prepare themselves for butanol challenge before butanol is produced, leading to an increased butanol yield. This is the first report on the comparative proteome analysis of a mutant strain and a base strain of C. acetobutylicum. The fundamental proteomic data and analyses will be useful for further elucidating the biological mechanism of butanol tolerance and/or enhanced butanol production.
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