Cytosolic events involved in chloroplast protein targeting
SCIE
SCOPUS
- Title
- Cytosolic events involved in chloroplast protein targeting
- Authors
- Lee, DW; Jung, C; Hwang, I
- Date Issued
- 2013-02
- Publisher
- ELSEVIER SCIENCE BV
- Abstract
- Chloroplasts are unique organelles that are responsible for photosynthesis. Although chloroplasts contain their own genome, the majority of chloroplast proteins are encoded by the nuclear genome. These proteins are transported to the chloroplasts after translation in the cytosol. Chloroplasts contain three membrane systems (outer/inner envelope and thylakoid membranes) that subdivide the interior into three soluble compartments known as the intermembrane space, stroma, and thylakoid lumen. Several targeting mechanisms are required to deliver proteins to the correct chloroplast membrane or soluble compartment. These mechanisms have been extensively studied using purified chloroplasts in vitro. Prior to targeting these proteins to the various compartments of the chloroplast, they must be correctly sorted in the cytosol. To date, it is not clear how these proteins are sorted in the cytosol and then targeted to the chloroplasts. Recently, the cytosolic carrier protein AKR2 and its associated cofactor Hsp17.8 for outer envelope membrane proteins of chloroplasts were identified. Additionally, a mechanism for controlling unimported plastid precursors in the cytosol has been discovered. This review will mainly focus on recent findings concerning the possible cytosolic events that occur prior to protein targeting to the chloroplasts. This article is part of a Special Issue entitled: Protein Import and Quality Control in Mitochondria and Plastids. (C) 2012 Elsevier B.V. All rights reserved.
- Keywords
- Chloroplast targeting signal; Cytosolic import factors; Outer envelope membrane; Chloroplast precursors in cytosol; SIGNAL RECOGNITION PARTICLE; OUTER-MEMBRANE PROTEINS; IMPORT STIMULATION FACTOR; PLASTID TRANSIT PEPTIDES; E3 UBIQUITIN LIGASE; ENDOPLASMIC-RETICULUM; PRECURSOR PROTEINS; TRANSMEMBRANE DOMAIN; ENVELOPE MEMBRANE; SEQUENCE MOTIFS
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/16363
- DOI
- 10.1016/J.BBAMCR.2012.03.006
- ISSN
- 0167-4889
- Article Type
- Article
- Citation
- BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, vol. 1833, no. 2, page. 245 - 252, 2013-02
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