TY  - JOUR
A1  - Groß, Lucia E.
A1  - Spies, Nicole
A1  - Simm, Stefan
A1  - Schleiff, Enrico
T1  - Toc75‐V/OEP80 is processed during translocation into chloroplasts, and the membrane‐embedded form exposes its POTRA domain to the intermembrane space
T2  - FEBS Open Bio
N2  - The insertion of membrane proteins requires proteinaceous complexes in the cytoplasm, the membrane, and the lumen of organelles. Most of the required complexes have been described, while the components for insertion of β‐barrel‐type proteins into the outer membrane of chloroplasts remain unknown. The same holds true for the signals required for the insertion of β‐barrel‐type proteins. At present, only the processing of Toc75‐III, the β‐barrel‐type protein of the central chloroplast translocon with an atypical signal, has been explored in detail. However, it has been debated whether Toc75‐V/ outer envelope protein 80 (OEP80), a second protein of the same family, contains a signal and undergoes processing. To substantiate the hypothesis that Toc75‐V/OEP80 is processed as well, we reinvestigated the processing in a protoplast‐based assay as well as in native membranes. Our results confirm the existence of a cleavable segment. By protease protection and pegylation, we observed intermembrane space localization of the soluble N‐terminal domain. Thus, Toc75‐V contains a cleavable N‐terminal signal and exposes its polypeptide transport‐associated domains to the intermembrane space of plastids, where it likely interacts with its substrates.
KW  - chloroplasts
KW  - OEP80
KW  - protein import
KW  - protein membrane insertion
KW  - Toc75-V
KW  - b-barrel membrane protein
Y1  - 2020
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/52885
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-528857
SN  - 2211-5463
N1  - FEBS Open Bio (2020) © 2020 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
VL  - 10
SP  - 1
EP  - 11
PB  - Elsevier on behalf of the Federation of European Biochemical Societies
CY  - Cambridge
ER  -