Negatively charged phospholipids trigger the interaction of a bacterial tat substrate precursor protein with lipid monolayers

verfasst von

Tina Brehmer, Andreas Kerth, Wenke Graubner, Miroslav Malesevic, Bo Hou, Thomas Brüser, Alfred Blume

Abstract

Folded proteins can be translocated across biological membranes via the Tat machinery. It has been shown in vitro that these Tat substrates can interact with membranes prior to translocation. Here we report a monolayer and infrared reflection-absorption spectroscopic (IRRAS) study of the initial states of this membrane interaction, the binding to a lipid monolayer at the air/water interface serving as a model for half of a biological membrane. Using the model Tat substrate HiPIP (high potential iron-sulfur protein) from Allochromatium vinosum, we found that the precursor preferentially interacts with monolayers of negatively charged phospholipids. The signal peptide is essential for the interaction of the precursor protein with the monolayer because the mature HiPIP protein showed no interaction with the lipid monolayer. However, the individual signal peptide interacted differently with the monolayer compared to the complete precursor protein. IRRA spectroscopy indicated that the individual signal peptide forms mainly aggregated β-sheet structures. This β-sheet formation did not occur for the signal peptide when being part of the full length precursor. In this case it adopted an ?-helical structure upon membrane insertion. The importance of the signal peptide and the mature domain for the membrane interaction is discussed in terms of current ideas of Tat substrate-membrane interactions.

Organisationseinheit(en)

Institut für Mikrobiologie

Externe Organisation(en)

Martin-Luther-Universität Halle-Wittenberg
Max-Planck-Forschungsstelle für Enzymologie der Proteinfaltung

Typ

Artikel

Journal

LANGMUIR

Band

28

Seiten

3534-3541

Anzahl der Seiten

8

ISSN

0743-7463

Publikationsdatum

21.02.2012

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Werkstoffwissenschaften (insg.), Physik der kondensierten Materie, Oberflächen und Grenzflächen, Spektroskopie, Elektrochemie

Elektronische Version(en)

https://doi.org/10.1021/la204473t (Zugang: Unbekannt)