Import of preproteins into the chloroplast inner envelope membrane

Import of preproteins into the chloroplast inner envelope membrane The chloroplast inner envelope membrane contains many integral proteins which differ in the number of α-helices that anchor the protein into the bilayer. For most of these proteins it is not known which pathway they engage to reach their final localisation within the membrane. In yeast mitochondria, two distinct sorting/insertion pathways have been described for integral inner membrane proteins, involving the Tim22 and Tim23 translocases. These routes involve on the one hand a conservative sorting, on the other hand a stop-transfer pathway. In this study we performed a systematic characterisation of the import behaviour of seven inner envelope proteins representing different numbers of predicted α-helices. We investigated their energy dependence, import rate, involvement of components of the chloroplast general import pathway and distribution between soluble and membrane fractions. Our results show the existence of at least two different families of inner envelope proteins that can be classified due to the occurrence of an intermediate processing form. Each of the proteins we investigated seems to use a stop-transfer pathway for insertion into the inner envelope. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Import of preproteins into the chloroplast inner envelope membrane

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Publisher
Springer Netherlands
Copyright
Copyright © 2008 by Springer Science+Business Media B.V.
Subject
Life Sciences; Plant Pathology; Biochemistry, general; Plant Sciences
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1007/s11103-008-9387-4
Publisher site
See Article on Publisher Site

Abstract

The chloroplast inner envelope membrane contains many integral proteins which differ in the number of α-helices that anchor the protein into the bilayer. For most of these proteins it is not known which pathway they engage to reach their final localisation within the membrane. In yeast mitochondria, two distinct sorting/insertion pathways have been described for integral inner membrane proteins, involving the Tim22 and Tim23 translocases. These routes involve on the one hand a conservative sorting, on the other hand a stop-transfer pathway. In this study we performed a systematic characterisation of the import behaviour of seven inner envelope proteins representing different numbers of predicted α-helices. We investigated their energy dependence, import rate, involvement of components of the chloroplast general import pathway and distribution between soluble and membrane fractions. Our results show the existence of at least two different families of inner envelope proteins that can be classified due to the occurrence of an intermediate processing form. Each of the proteins we investigated seems to use a stop-transfer pathway for insertion into the inner envelope.

Journal

Plant Molecular BiologySpringer Journals

Published: Aug 14, 2008

References

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