scholarly journals Identification of a Signal That Distinguishes between the Chloroplast Outer Envelope Membrane and the Endomembrane System in Vivo

2001 ◽  
Vol 13 (10) ◽  
pp. 2175-2190 ◽  
Author(s):  
Yong Jik Lee ◽  
Dae Heon Kim ◽  
Yong-Woo Kim ◽  
Inhwan Hwang
Keyword(s):  
Envelope Membrane ◽  
Endomembrane System ◽  
Outer Envelope ◽  
Outer Envelope Membrane

scholarly journals In Vivo Analyses of the Roles of Essential Omp85-Related Proteins in the Chloroplast Outer Envelope Membrane

2011 ◽  
Vol 157 (1) ◽  
pp. 147-159 ◽  
Author(s):  
Weihua Huang ◽  
Qihua Ling ◽  
Jocelyn Bédard ◽  
Kathryn Lilley ◽  
Paul Jarvis
Keyword(s):  
Envelope Membrane ◽  
Outer Envelope ◽  
Outer Envelope Membrane ◽  
Related Proteins

scholarly journals Insertion of plastidic β-barrel proteins into the outer envelopes of plastids involves an intermembrane space intermediate formed with Toc75-V/OEP80

2021 ◽  
Author(s):  
Lucia E Gross ◽  
Anna Klinger ◽  
Nicole Spies ◽  
Theresa Ernst ◽  
Nadine Flinner ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Protein Import ◽  
Membrane Insertion ◽  
Intermembrane Space ◽  
Envelope Membrane ◽  
Outer Envelope ◽  
Pea Proteins ◽  
Outer Envelope Membrane ◽  
Correct Topology ◽  
Shed Light

Abstract The insertion of organellar membrane proteins with the correct topology requires the following: First, the proteins must contain topogenic signals for translocation across and insertion into the membrane. Second, proteinaceous complexes in the cytoplasm, membrane, and lumen of organelles are required to drive this process. Many complexes required for the intracellular distribution of membrane proteins have been described, but the signals and components required for the insertion of plastidic β-barrel-type proteins into the outer membrane are largely unknown. The discovery of common principles is difficult, as only a few plastidic β-barrel proteins exist. Here, we provide evidence that the plastidic outer envelope β-barrel proteins OEP21, OEP24, and OEP37 from pea (Pisum sativum) and Arabidopsis thaliana contain information defining the topology of the protein. The information required for translocation of pea proteins across the outer envelope membrane is present within the six N-terminal β-strands. This process requires the action of TOC (translocon of the outer chloroplast membrane). After translocation into the intermembrane space, β-barrel proteins interact with TOC75-V, as exemplified by OEP37 and P39, and are integrated into the membrane. The membrane insertion of plastidic β-barrel proteins is affected by mutation of the last β-strand, suggesting that this strand contributes to the insertion signal. These findings shed light on the elements and complexes involved in plastidic β-barrel protein import.

Mechanism of protein import across the chloroplast envelope

2000 ◽  
Vol 28 (4) ◽  
pp. 485-491 ◽  
Author(s):  
K. Chen ◽  
X. Chen ◽  
D. J. Schnell
Keyword(s):  
Protein Import ◽  
Essential Elements ◽  
Chloroplast Envelope ◽  
Envelope Membrane ◽  
Outer Envelope ◽  
Double Membrane ◽  
Protein Subunits ◽  
Targeting Signals ◽  
Outer Envelope Membrane ◽  
Envelope Membranes

The development and maintenance of chloroplasts relies on the contribution of protein subunits from both plastid and nuclear genomes. Most chloroplast proteins are encoded by nuclear genes and are post-translationally imported into the organelle across the double membrane of the chloroplast envelope. Protein import into the chloroplast consists of two essential elements: the specific recognition of the targeting signals (transit sequences) of cytoplasmic preproteins by receptors at the outer envelope membrane and the subsequent translocation of preproteins simultaneously across the double membrane of the envelope. These processes are mediated via the co-ordinate action of protein translocon complexes in the outer (Toe apparatus) and inner (Tic apparatus) envelope membranes.

Detection of small GTP-binding proteins in the outer envelope membrane of pea chloroplasts

1992 ◽  
pp. 209-212
Author(s):  
Yukio Nagano ◽  
Kazumasa Sekiguchi ◽  
Nobuhiko Mural ◽  
Ryuichi Matsuno ◽  
Yukiko Sasaki
Keyword(s):  
Binding Proteins ◽  
Envelope Membrane ◽  
Outer Envelope ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Outer Envelope Membrane

scholarly journals Spinach hexokinase I is located in the outer envelope membrane of plastids

FEBS Letters ◽  
1999 ◽  
Vol 461 (1-2) ◽  
pp. 13-18 ◽  
Author(s):  
Anika Wiese ◽  
Ferdi Gröner ◽  
Uwe Sonnewald ◽  
Heike Deppner ◽  
Jens Lerchl ◽  
...  
Keyword(s):  
Envelope Membrane ◽  
Outer Envelope ◽  
Outer Envelope Membrane

scholarly journals Synthesis and transfer of galactolipids in the chloroplast envelope membranes of Arabidopsis thaliana

2016 ◽  
Vol 113 (38) ◽  
pp. 10714-10719 ◽  
Author(s):  
Amélie A. Kelly ◽  
Barbara Kalisch ◽  
Georg Hölzl ◽  
Sandra Schulze ◽  
Juliane Thiele ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
Chloroplast Envelope ◽  
Envelope Membrane ◽  
Lipid Transfer ◽  
Terminal Sequence ◽  
Outer Envelope ◽  
Outer Envelope Membrane ◽  
Envelope Reconstruction ◽  
Envelope Membranes

Galactolipids [monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG)] are the hallmark lipids of photosynthetic membranes. The galactolipid synthases MGD1 and DGD1 catalyze consecutive galactosyltransfer reactions but localize to the inner and outer chloroplast envelopes, respectively, necessitating intermembrane lipid transfer. Here we show that the N-terminal sequence of DGD1 (NDGD1) is required for galactolipid transfer between the envelopes. Different diglycosyllipid synthases (DGD1, DGD2, and Chloroflexus glucosyltransferase) were introduced into the dgd1-1 mutant of Arabidopsis in fusion with N-terminal extensions (NDGD1 and NDGD2) targeting to the outer envelope. Reconstruction of DGDG synthesis in the outer envelope membrane was observed only with diglycosyllipid synthase fusion proteins carrying NDGD1, indicating that NDGD1 enables galactolipid translocation between envelopes. NDGD1 binds to phosphatidic acid (PA) in membranes and mediates PA-dependent membrane fusion in vitro. These findings provide a mechanism for the sorting and selective channeling of lipid precursors between the galactolipid pools of the two envelope membranes.

Sign in / Sign up

Export Citation Format

Share Document