INVESTIGADORES
RODRIGUEZ Fernanda Mariana
congresos y reuniones científicas
Título:
Study of Escherichia coli TatA
Autor/es:
FERNANDA RODRIGUEZ; JASON SCHNELL; BEN C. BERKS
Lugar:
Munich
Reunión:
Congreso; SFB Meeting: Molecular Machines in Protein Folding and Transport; 2012
Resumen:
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In the Tat pathway, proteins are
translocated fully folded across the cell membrane. The Tat pathway is found in
bacteria, archaea and plant chloroplasts, and is required for important
bacterial cellular processes including respiratory and photosynthetic energy
metabolism, cell division, cell motility, quorum sensing, heavy metal
resistance, iron acquisition, and biofilm formation. In E. coli, Tat consists of three components: TatA, TatB, and TatC.
Experimental evidence suggests that a TatBC complex binds to the signal peptide
of the substrate protein. This binding event triggers the assembly of TatA with
the TatBC-substrate complex, and the substrate protein is then translocated
probably via TatA. TatA is an 89-residue protein comprising an N-terminal
transmembrane helix, followed by an amphipathic helix, and an unstructured and
hydrophilic cytoplasmic tail. TatA is currently considered to form tetramers
that act as building blocks for the higher-order oligomers that mediate
transport. The higher-order polymerisation of TatA is dynamic and thought to be
biased by substrate-bound TatBC. In this work we report the results of
structural studies by NMR spectroscopy performed on E. coli TatA aimed at unveiling its molecular mechanism of action.