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Protein polymerization via 3D domain swapping has been suggested to promote amyloid plaque formation. Two recent papers provide support for a role for domain swapping in the formation of highly ordered aggregates such as the fibrils characteristic of amyloid plaques.
The protein translocation channel of the outer mitochondrial membrane is thought to be a rigid β-barrel. Newly synthesized membrane proteins apparently do not escape laterally from this channel into the lipid bilayer, but must insert into the outer membrane from the aqueous phase. A study on the biogenesis of the mitochondrial outer membrane translocation machinery now shows that the subunit forming the protein import channel is first translocated across the outer membrane and then reinserted.
Recent crystallographic analyses of membrane-tethering FYVE finger domains from proteins involved in the regulation of endocytic vesicle trafficking have led to conflicting views of the precise nature of the contacts formed with the specific phospholipid ligand. New NMR data obtained for ligand-bound forms of a FYVE domain help resolve the atomic details of this interaction.
Crystal structures of the homing endonuclease I-CreI bound to substrate DNA and divalent metals show that one metal ion is shared between the two active sites of the enzyme. This arrangement appears uniquely suited to the formation of double-stranded DNA breaks via a concerted reaction.
In the ATP-dependent proteases, separate internal chambers function in substrate unfolding and degradation. These chambers are linked by narrow channels, requiring a protein to unfold completely in order to pass between them. New work suggests that substrates are unraveled from one end first and are translocated vectorially into the proteolytic core.
Telomeres, the protein–DNA complexes at the ends of eukaryotic chromosomes, are essential for chromosomal stability. Recent findings suggest that a single regulator in yeast, Cdc13, nucleates specific subcomplexes that regulate specific telomeric functions.
