Epoxydeacetylcytochalasin H

The TORC1 (Target of Rapamycin Complex 1) kinase complex plays a pivotal role in controlling cell growth in probably all eukaryotic species. The signals and mechanisms regulating TORC1 have been intensely studied in mammals but those of fungi and plants are much less known. We have previously reported that the yeast plasma membrane H+-ATPase Pma1 promotes TORC1 activation when stimulated by cytosolic acidification or nutrient-uptake-coupled H+ influx. Furthermore, a homologous plant H+-ATPase can substitute for yeast Pma1 to promote this H+-elicited TORC1 activation. We here report that TORC1 activity in Nicotiana tabacum BY-2 cells is also strongly influenced by the activity of plasma membrane H+-ATPases. In particular, stimulation of H+-ATPases by fusicoccin activates TORC1, and this response is also observed in cells transferred to a nutrient-free and auxin-free medium. Our results suggest that plant H+-ATPases, known to be regulated by practically all factors controlling cell growth, contribute to TOR signaling.

Distal C(sp2 )-H and C(sp3 )-H functionalizations have recently emerged as step-economical tools for molecular synthesis. However, while the C(sp2 )-C(sp3 ) construction is of fundamental importance, its formation through double remote C(sp2 )-H/C(sp3 )-H activation has proven elusive. By merging the ruthenium-catalyzed meta-C(sp2 )-H functionalization with an aliphatic hydrogen atom transfer (HAT) process, we, herein, describe the catalyzed twofold remote C(sp2 )-H/C(sp3 )-H functionalizations via photo-induced ruthenium-mediated radical relay. Thus, meta-C(sp2 )-H arene bonds and remote C(sp3 )-H alkane bonds were activated by a single catalyst in a single operation. This process was accomplished at room temperature by visible light-notably without exogenous photocatalysts. Experimental and computational theory studies uncovered a manifold comprising ortho-C-H activation, single-electron-transfer (SET), 1,n-HAT (n=5-7) and σ-activation by means of a single ruthenium(II) catalyst.

In plants, cytosolic and extracellular pH homeostasis are crucial for various physiological processes, including the uptake of macronutrients and micronutrients, cell elongation, cell expansion, and enzyme activity. Proton (H+) gradients and the membrane potential are generated by a H+ pump consisting of an active primary transporter. Plasma membrane (PM) H+-ATPase, a PM-localized H+ pump, plays a pivotal role in maintaining pH homeostasis in plant cells and extracellular regions. PM H+-ATPase activity is regulated by protein abundance and by post-translational modifications. Several stimuli have been found to activate the PM H+-ATPase through phosphorylation of the penultimate threonine (Thr) of the carboxy terminus. Light- and photosynthesis-induced phosphorylation of PM H+-ATPase are conserved phenomena among various plant species. In this work, we review recent findings related to PM H+-ATPase regulation in the photosynthetic tissues of plants, focusing on its mechanisms and physiological roles. The physiological roles of photosynthesis-dependent PM H+-ATPase activation are discussed in the context of nitrate uptake and cytoplasmic streaming in leaves.