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Stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2
Plastoglobules (PGs) are plastidial lipid droplets enclosed by a polar monolayer born from the thylakoid membrane when plants require active lipid metabolism, including carotenogenesis, under the environmental stress and during plastid transition. Despite the fact that many proteins are reported to...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10264786/ https://www.ncbi.nlm.nih.gov/pubmed/37324722 http://dx.doi.org/10.3389/fpls.2023.1181311 |
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author | Yu, Ji Su You, Min Kyoung Lee, Yeo Jin Ha, Sun-Hwa |
author_facet | Yu, Ji Su You, Min Kyoung Lee, Yeo Jin Ha, Sun-Hwa |
author_sort | Yu, Ji Su |
collection | PubMed |
description | Plastoglobules (PGs) are plastidial lipid droplets enclosed by a polar monolayer born from the thylakoid membrane when plants require active lipid metabolism, including carotenogenesis, under the environmental stress and during plastid transition. Despite the fact that many proteins are reported to target PGs, their translocation mechanism has remained largely unexplored. To elucidate this process, we studied the influence of three hydrophobic regions (HR)—HR1 (1–45(th) aa), HR2 (46–80(th) aa), and HR3 (229–247(th) aa)—of rice phytoene synthase 2 (OsPSY2, 398 aa), which has previously shown to target PGs. As results, HR1 includes the crucial sequence (31–45(th) aa) for chloroplast import and the stromal cleavage occurs at a specific alanine site (64(th) aa) within HR2, verifying that a N-terminal 64-aa-region works as the transit peptide (Tp). HR2 has a weak PG-targeting signal by showing synchronous and asynchronous localization patterns in both PGs and stroma of chloroplasts. HR3 exhibited a strong PG-targeting role with the required positional specificity to prevent potential issues such as non-accumulation, aggregation, and folding errors in proteins. Herein, we characterized a Tp and two transmembrane domains in three HRs of OsPSY2 and propose a spontaneous pathway for its PG-translocation with a shape embedded in the PG-monolayer. Given this subplastidial localization, we suggest six sophisticated tactics for plant biotechnology applications, including metabolic engineering and molecular farming. |
format | Online Article Text |
id | pubmed-10264786 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-102647862023-06-15 Stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2 Yu, Ji Su You, Min Kyoung Lee, Yeo Jin Ha, Sun-Hwa Front Plant Sci Plant Science Plastoglobules (PGs) are plastidial lipid droplets enclosed by a polar monolayer born from the thylakoid membrane when plants require active lipid metabolism, including carotenogenesis, under the environmental stress and during plastid transition. Despite the fact that many proteins are reported to target PGs, their translocation mechanism has remained largely unexplored. To elucidate this process, we studied the influence of three hydrophobic regions (HR)—HR1 (1–45(th) aa), HR2 (46–80(th) aa), and HR3 (229–247(th) aa)—of rice phytoene synthase 2 (OsPSY2, 398 aa), which has previously shown to target PGs. As results, HR1 includes the crucial sequence (31–45(th) aa) for chloroplast import and the stromal cleavage occurs at a specific alanine site (64(th) aa) within HR2, verifying that a N-terminal 64-aa-region works as the transit peptide (Tp). HR2 has a weak PG-targeting signal by showing synchronous and asynchronous localization patterns in both PGs and stroma of chloroplasts. HR3 exhibited a strong PG-targeting role with the required positional specificity to prevent potential issues such as non-accumulation, aggregation, and folding errors in proteins. Herein, we characterized a Tp and two transmembrane domains in three HRs of OsPSY2 and propose a spontaneous pathway for its PG-translocation with a shape embedded in the PG-monolayer. Given this subplastidial localization, we suggest six sophisticated tactics for plant biotechnology applications, including metabolic engineering and molecular farming. Frontiers Media S.A. 2023-05-31 /pmc/articles/PMC10264786/ /pubmed/37324722 http://dx.doi.org/10.3389/fpls.2023.1181311 Text en Copyright © 2023 Yu, You, Lee and Ha https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Yu, Ji Su You, Min Kyoung Lee, Yeo Jin Ha, Sun-Hwa Stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2 |
title | Stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2 |
title_full | Stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2 |
title_fullStr | Stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2 |
title_full_unstemmed | Stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2 |
title_short | Stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2 |
title_sort | stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2 |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10264786/ https://www.ncbi.nlm.nih.gov/pubmed/37324722 http://dx.doi.org/10.3389/fpls.2023.1181311 |
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