Premium
Electrostatics and Intrinsic Disorder Drive Translocon Binding of the SRP Receptor FtsY
Author(s) -
Lakomek NilsAlexander,
Draycheva Albena,
Bornemann Thomas,
Wintermeyer Wolfgang
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201602905
Subject(s) - translocon , biophysics , signal recognition particle , signal recognition particle receptor , chemistry , biology , membrane protein , protein targeting , microbiology and biotechnology , biochemistry , membrane , signal peptide , peptide sequence , gene
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.