Rui Sousa

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Assembly of clathrin lattices is mediated by assembly/adaptor proteins that contain domains that bind lipids or membrane-bound cargo proteins and clathrin binding domains (CBDs) that recruit clathrin. Here, we characterize the interaction between clathrin and a large fragment of the CBD of the clathrin assembly protein AP180. Mutational, NMR chemical shift,(More)
Neurotransmission requires a continuously available pool of synaptic vesicles (SVs) that can fuse with the plasma membrane and release their neurotransmitter contents upon stimulation. After fusion, SV membranes and membrane proteins are retrieved from the presynaptic plasma membrane by clathrin-mediated endocytosis. After the internalization of a(More)
Time-resolved characterization of T7 RNA polymerase pausing and terminating at a class II termination site has been carried out using site-specifically tethered chemical nucleases. The data indicate that T7RNAP normally moves uniformly down the template as a rigid body. However, at the class II site this movement is interrupted, and the leading edge of the(More)
During transcription initiation, RNA polymerases appear to retain promoter interactions while transcribing short RNAs that are frequently released from the complex. Upon transition to elongation, the polymerase releases promoter and forms a stable elongation complex. Little is known about the changes in polymerase conformation or polymerase:DNA interactions(More)
Ahmad et al. recently presented an NMR-based model for a bacterial DnaJ J domain:DnaK(Hsp70):ADP complex(1) that differs significantly from the crystal structure of a disulfide linked mammalian auxilin J domain:Hsc70 complex that we previously published(2). They claimed that their model could better account for existing mutational data, was in better(More)
The mechanisms by which RNA polymerase moves along DNA during elongation have been difficult to determine experimentally. In this issue of Cell, Bar-Nahum et al. (2005) show that back and forth sliding of RNA polymerase on DNA may be coupled to bending of an alpha helix, which can alternately occlude and expose the NTP binding site. Transcription factors(More)