scholarly journals Analysis of Pea Chloroplast Inner and Outer Envelope Membrane Proteins by Two-Dimensional Gel Electrophoresis and Their Comparison with Stromal Proteins

1983 ◽  
Vol 73 (3) ◽  
pp. 569-575 ◽  
Author(s):  
Margaret Werner-Washburne ◽  
Kenneth Cline ◽  
Kenneth Keegstra
Keyword(s):  
Membrane Proteins ◽  
Gel Electrophoresis ◽  
Envelope Membrane ◽  
Two Dimensional ◽  
Outer Envelope ◽  
Two Dimensional Gel Electrophoresis ◽  
Outer Envelope Membrane ◽  
Stromal 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.

Preparative two-dimensional gel electrophoresis of membrane proteins

1997 ◽  
Vol 18 (14) ◽  
pp. 2573-2581 ◽  
Author(s):  
Christian Pasquali ◽  
Irene Fialka ◽  
Lukas A. Huber
Keyword(s):  
Membrane Proteins ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Biogenesis of chloroplast outer envelope membrane proteins

2019 ◽  
Vol 38 (7) ◽  
pp. 783-792 ◽  
Author(s):  
Jonghak Kim ◽  
Yun Jeong Na ◽  
Soon Ju Park ◽  
So-Hyeon Baek ◽  
Dae Heon Kim
Keyword(s):  
Membrane Proteins ◽  
Envelope Membrane ◽  
Outer Envelope ◽  
Outer Envelope Membrane

Exploitation of detergent thermodynamics in the direct solubilization of myelin membrane proteins for two-dimensional gel electrophoresis for proteomic analysis

2011 ◽  
Vol 32 (24) ◽  
pp. 3621-3629 ◽  
Author(s):  
Sreepriya Nair ◽  
Tessy Xavier ◽  
Madathiparambil Kumaran Satheesh Kumar ◽  
Sharmistha Saha ◽  
Krishnakumar N. Menon
Keyword(s):  
Membrane Proteins ◽  
Proteomic Analysis ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Myelin Membrane

Preparation of membrane proteins for analysis by two-dimensional gel electrophoresis

2007 ◽  
Vol 849 (1-2) ◽  
pp. 282-292 ◽  
Author(s):  
Yasuhiro Kashino ◽  
Takeshi Harayama ◽  
Himadri B. Pakrasi ◽  
Kazuhiko Satoh
Keyword(s):  
Membrane Proteins ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis
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