Details

Autor(en) / Beteiligte

• Lakomek, Nils-Alexander
• Draycheva, Albena
• Bornemann, Thomas
• Wintermeyer, Wolfgang

Titel

Electrostatics and Intrinsic Disorder Drive Translocon Binding of the SRP Receptor FtsY

Ist Teil von

• Angewandte Chemie (International ed.), 2016-08, Vol.55 (33), p.9544-9547

Auflage

International ed. in English

Ort / Verlag

Germany: Blackwell Publishing Ltd

Erscheinungsjahr

2016

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• 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. Integral membrane proteins in bacteria are co‐translationally targeted to the 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. Translocon targeting and binding of FtsY is driven by electrostatic interactions of the intrinsically disordered A domain.