| Summary: | Translocation of proteins into or across the lipid bilayer is an essential process for all
living cells. The Sec translocon, known as Sec61αγβ in eukaryotes and SecYEG in prokaryotes,
is composed of three subunits in which the largest one, Sec61α or SecY, constitutes the protein
channel or pore in the membrane. For the majority of integral membrane proteins, translocation
is performed through the signal recognition particle (SRP) pathway. In this pathway, the SRP
recognizes and binds to the leading signal sequence of nascent proteins emerging from
translating ribosomal units. Through an interaction with an SRP receptor (SR), located at the
membrane, the SRP-ribosome-nascent chain complex is brought to close proximity of the Sec
complex.
In this thesis, the interaction between the prokaryotic SRP receptor, FtsY, and the
SecYEG complex is analyzed. The A domain of FtsY is identified as the SecYEG-FtsY
interacting domain by Blue Native PAGE and analytical gel filtration. Using surface plasmon
resonance technique, the binding affinity of FtsY to the Sec translocon is measured. Finally, the
interaction seems to inhibit the GTPase activity of FtsY. === Medicine, Faculty of === Biochemistry and Molecular Biology, Department of === Graduate
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