Biochemistry Research Track

1. Electron microscopic reconstruction of the flagellar basal body, from DeRosier and coworkers (J. Bacteriol. 188, 7039-48). The structure is viewed from the side. The bottom-most feature, termed the C-ring, is in the cytosol. A working hypothesis for the locations of the FliG, FliM and FliN proteins is shown at the right of the C-ring.
2. Detail showing rings of density at the bottom of the C-ring.
3. The appearance of the bottom of the C-ring as determined by EM, and the organization of FliN and FliM proteins deduced from cross-linking and mutational studies.

One mitochondrial OXPHOS respirasome is a supercomplex consisting of Complexes I, III and IV. Electrons from the oxidation of NADH are shuttled through the complexes to Complex IV for the reduction of molecular oxygen.

Nhp6 binds to DNA at multiple sites in a nucleosome, weakening the protein-DNA contacts. Spt16-Pob3 dimers further destabilize the nucleosome to an alternative "reorganized" form, providing access to DNA within chromatin.

Crystal structure of PIE12 binding to IQN17. Trp35 of the gp41 pocket and the N-terminal flank residues of PIE12 (His3 and Pro4) appear to stabilize binding via ring-stacking interactions.