Marina Diskowski, Ahmad Reza Mehdipour ... Inga Hänelt
The K(+) uptake system KtrAB is controlled by an allosteric mechanism entirely new for membrane channels, which operates the channel gate over a 35 Å distance.
The structure of the VemP-stalled ribosome reveals a helix-double turn-helix conformation of the nascent chain within the ribosomal tunnel, illustrating how secondary structure formation directly at the peptidyltransferase center of the ribosome can induce translational arrest.
Joshua J Filter, Byron C Williams ... Michael L Goldberg
Unfair competition, in which a phosphatase and a phosphoprotein inhibitor/substrate mutually sequester each other from competing substrates and enzymes, is a conserved mechanism for the control of PPP family phosphatases.
The Srs2 helicase functions in Synthesis-Dependent Strand Annealing to avoid crossover formation during homologous recombination by disrupting D-loops that are extended by DNA polymerase delta in an ATP-dependent and direction-specific manner.
Adam Graham Grieve, Hongmei Xu ... Matthew Freeman
The iRhom2 protein, a catalytically inactive relative of rhomboid proteases, controls inflammation and growth factor signalling by acting as an essential multifunctional regulatory subunit of the cell surface shedding protease TACE (ADAM17).
A post-lysosomal cholesterol transport inhibitor reveals how the endoplasmic reticulum membrane regulates total cellular cholesterol by constantly monitoring a critical pool of cholesterol in the plasma membrane.
Sven Kenjiro Vogel, Ferdinand Greiss ... Petra Schwille
Building on previous work (Vogel et al., 2013b), it is shown that myosin-driven actin filament rearrangements actively move, split or fuse individual lipid domains and change their overall shape.
See-Yeun Ting, Nicholas L Yan ... Elizabeth A Craig
The motor that drives preproteins into the mitochondrial matrix is coupled to the translocase by Tim44, a two-domain scaffold protein with an intrinsically disordered "dynamic arm" and a structurally stable anchoring domain.