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Chloroplasts, distinctive subcellular organelles found exclusively in plant species, contain three membranes: the outer, inner, and thylakoid membranes. They also have three soluble compartments: the intermembrane space, stroma, and thylakoid lumen. Accordingly, delicate sorting mechanisms are required to ensure proper protein targeting to these sub-chloroplast compartments. Except for most outer membrane proteins, chloroplast interior proteins possess N-terminal cleavable transit peptides as primary import signals. After the cleavage of transit peptides, which occurs during or after import into chloroplasts, the inner and thylakoid membrane proteins, as well as stromal and thylakoid luminal proteins, are further sorted based on additional targeting signals. In this review, we aim to recapitulate the mechanisms by which proteins are targeted to chloroplasts and subsequently sorted into sub-chloroplast compartments, with a focus on the design principles of sorting signals present in chloroplast proteins.
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http://dx.doi.org/10.1007/s00299-024-03409-2 | DOI Listing |
Plant Cell Rep
December 2024
Department of Integrative Food, Bioscience and Biotechnology, Chonnam National University, Gwangju, 61186, South Korea.
Chloroplasts, distinctive subcellular organelles found exclusively in plant species, contain three membranes: the outer, inner, and thylakoid membranes. They also have three soluble compartments: the intermembrane space, stroma, and thylakoid lumen. Accordingly, delicate sorting mechanisms are required to ensure proper protein targeting to these sub-chloroplast compartments.
View Article and Find Full Text PDFMicron
June 2021
Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, 310021, China. Electronic address:
Quantification of immuno-gold labeling can provide valuable information on the quantity and localization of a target within a region of interest (ROI). Background subtraction usually requires preparation of material with a deliberately reduced amount of target component often by gene knockout/knockdown. This paper reports a modified method without the need for gene knockout/knockdown, by using a region outside the ROI as a background and non-immune serum to verify the reliability of the data.
View Article and Find Full Text PDFMethods Mol Biol
November 2011
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Chloroplasts have one of the most complicated structures among organelles. They have three membrane systems, the outer and inner envelope membranes and the thylakoid membrane, which enclose three aqueous spaces: the intermembrane space between the two envelope membranes, the stroma, and the thylakoid lumen. Each of the chloroplast's sub-organellar compartments houses a distinct set of proteins that perform distinct functions.
View Article and Find Full Text PDFPhotosynth Res
September 1991
Robert Hill Institute of Photosynthesis, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, S10 2TN, Sheffield, UK.
Reversible changes in the room temperature fluorescence quenching at 685 nm and light scattering level at 577 nm, indicating about 15% of granal unstacking, induced by high temperature treatment (40°C, for 5 min) of pea chloroplasts were shown. Analysis of the low temperature excitation fluorescence spectra of the 735 nm Photosystem 1 (PS 1) band (F735), in the 635-725 nm region, has revealed the involvement of light-harvesting (LHC 2, maxima at 650 and 676 nm) and the proximal Photosystem 2 antenna (maxima 668, 687 nm) in heat-induced enhancement of the PS 1 long wavelength antenna absorption cross-section. It was found that the two PS 1 sub-chloroplast preparations, achieved by the digitonin method, possessed different characteristics of this enhancement.
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