In vitro studies on the SecA involvement in the assembly of an integral membrane protein with large hydrophilic domain [Elektronische Ressource] / vorgelegt von Raluca Antonoaea

In vitro studies on the SecA involvement in the assembly of an integral membrane protein with large hydrophilic domain INAUGURAL-DISSERTATION zur Erlangung der Doktorwürde der Fakultät der Biologie der Albert-Ludwigs-Universität Freiburg i.Br. vorgelegt von Raluca Antonoaea Piatra Neam ţ/Rumänien im November 2005 Dekan: Prof. Dr. Georg Fuchs Betreuer der Arbeit: Prof. Dr. Matthias Müller Promotionsvorsitzender: Prof. Dr. Samuel Rossel Koreferent: Prof. Dr. Gunther Neuhaus Wesentliche Teile der Arbeit wurden zur Publikation eingereicht: Raluca Antonoaea, Ken-ichi Nishiyama, Dominique Missiakas and Matthias Müller (2005) SecA Extrudes a Translocating Nascent Chain from the SecYEG Translocon Directly Onto the Periplasmic Chaperone PpiD Table of contents Table of contents I. Summary 1 II. Introduction 3 II.1. Protein transport in bacteria 3 II.2. Sec-dependent protein transport across the inner membrane of E. coli 4 II.2.1. Membrane protein recognition and targeting 5 II.2.1.1. Conservation of SRP 5 II.2.1.2. Interaction with the signal sequence 6 II.2.1.3. The mechanism of membrane protein targeting mediated by SRP/SR 7 II.2.2. Insertion of the integral membrane proteins in the SecYEG translocon 8 II.2.2.1.