C-terminal processing of yeast Spt7 occurs in the absence of functional SAGA complex

Background  

Spt7 is an integral component of the multi-subunit SAGA complex that is required for the expression of ~10% of yeast genes. Two forms of Spt7 have been identified, the second of which is truncated at its C-terminus and found in the SAGA-like (SLIK) complex.     

Cavitand zn(II)-porphyrin capsules with high affinities for pyridines and N-methylimidazole

Covalent cavitand Zn(II)-porphyrins 17-20 were prepared via multistep syntheses. These host molecules show moderate to excellent binding affinities to N-methylimidazole and pyridine guests. The complexing behavior strongly depends on the spacer's length, number, and rigidity, in addition to the guest size. Cavitand capping and strapping of porphyrins strongly influence the complex formation and result in a 10-700-fold enhancement of the binding strength compared to tetraphenyl Zn(II)-porphyrin.     

Bioactive cyclometalated phthalimides: design, synthesis and kinase inhibition

The regioselective cyclometalation of 4-(pyridin-2-yl)phthalimide was exploited for the economical design of organometallic protein kinase inhibitors. 4-(Pyridin-2-yl)phthalimide can be prepared from inexpensive 4-bromophthalimide in just three steps including one Pd-catalyzed Stille cross-coupling. The versatility of this new ligand was demonstrated with the synthesis of ruthenium(II) half-sandwich as well as octahedral ruthenium(II) and iridium(III) complexes. The regioselectivity of the C-H activation in the course of the cyclometalation can be influenced by the reaction conditions and the steric demand of the introduced metal complex fragment. The biological activity of this new class of metalated phthalimides was evaluated by profiling two representative members against a large panel of human protein kinases. A cocrystal structure of one metallo-phthalimide with the protein kinase Pim1 confirmed an ATP-competitive binding with the intended hydrogen bonding between the phthalimide moiety and the hinge region of the ATP-binding site.     

Surface stress anisotropy of Ge(001)

By analyzing the equilibrium shape of vacancy islands on the Ge(001) surface we have determined the surface stress anisotropy, i.e., the difference between the compressive stress component along the substrate dimer rows and the tensile stress component perpendicular to the substrate dimer rows. In order to extract the surface stress anisotropy we have used a model recently put forward by Li et al. [Phys. Rev. Lett. 85, 1922 (2000)]. The surface stress anisotropy of the clean Ge(001) surface is found to be 80+/-30 meV/A(2). This value is comparable to the surface stress anisotropy of the closely related Si(001) surface.