Electrostatics and intrinsic disorder drive translocon binding of the SRP 
receptor FtsY.

Lakomek, N. A.; Draycheva, A.; Bornemann, T.; Wintermeyer, W.

doi:10.1002/anie.201602905

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Electrostatics and intrinsic disorder drive translocon binding of the SRP receptor FtsY.

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Draycheva, A.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Bornemann, T.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Wintermeyer, W.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Lakomek, N. A., Draycheva, A., Bornemann, T., & Wintermeyer, W. (2016). Electrostatics and intrinsic disorder drive translocon binding of the SRP receptor FtsY. Angewandte Chemie International Edition, 55(33), 9544-9547. doi:10.1002/anie.201602905.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-F31C-6

Abstract

Integral membrane proteins in bacteria are co-translationally targeted to the SecYEG translocon for membrane insertion via the signal recognition particle (SRP) pathway. The SRP receptor FtsY and its N-terminal A domain, which is lacking in any structural model of FtsY, were studied using NMR and fluorescence spectroscopy. The A domain is mainly disordered and highly flexible; it binds to lipids via its N terminus and the C-terminal membrane targeting sequence. The central A domain binds to the translocon non-specifically and maintains disorder. Translocon targeting and binding of the A domain is driven by electrostatic interactions. The intrinsically disordered A domain tethers FtsY to the translocon, and because of its flexibility, allows the FtsY NG domain to scan a large area for binding to the NG domain of ribosome-bound SRP, thereby promoting the formation of the quaternary transfer complex at the membrane.