Cargando…
Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum
Protein bodies (PBs) are organelles found in seeds whose main function is the storage of proteins that are used during germination for sustaining growth. PBs can also be induced to form in leaves when foreign proteins are produced at high levels in the endoplasmic reticulum (ER) and when fused to on...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4876836/ https://www.ncbi.nlm.nih.gov/pubmed/27242885 http://dx.doi.org/10.3389/fpls.2016.00693 |
_version_ | 1782433297106731008 |
---|---|
author | Saberianfar, Reza Sattarzadeh, Amirali Joensuu, Jussi J. Kohalmi, Susanne E. Menassa, Rima |
author_facet | Saberianfar, Reza Sattarzadeh, Amirali Joensuu, Jussi J. Kohalmi, Susanne E. Menassa, Rima |
author_sort | Saberianfar, Reza |
collection | PubMed |
description | Protein bodies (PBs) are organelles found in seeds whose main function is the storage of proteins that are used during germination for sustaining growth. PBs can also be induced to form in leaves when foreign proteins are produced at high levels in the endoplasmic reticulum (ER) and when fused to one of three tags: Zera®, elastin-like polypeptides (ELP), or hydrophobin-I (HFBI). In this study, we investigate the differences between ELP, HFBI and Zera PB formation, packing, and communication. Our results confirm the ER origin of all three fusion-tag-induced PBs. We show that secretory pathway proteins can be sequestered into all types of PBs but with different patterns, and that different fusion tags can target a specific protein to different PBs. Zera PBs are mobile and dependent on actomyosin motility similar to ELP and HFBI PBs. We show in vivo trafficking of proteins between PBs using GFP photoconversion. We also show that protein trafficking between ELP or HFBI PBs is faster and proteins travel further when compared to Zera PBs. Our results indicate that fusion-tag-induced PBs do not represent terminally stored cytosolic organelles, but that they form in, and remain part of the ER, and dynamically communicate with each other via the ER. We hypothesize that the previously documented PB mobility along the actin cytoskeleton is associated with ER movement rather than independent streaming of detached organelles. |
format | Online Article Text |
id | pubmed-4876836 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-48768362016-05-30 Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum Saberianfar, Reza Sattarzadeh, Amirali Joensuu, Jussi J. Kohalmi, Susanne E. Menassa, Rima Front Plant Sci Plant Science Protein bodies (PBs) are organelles found in seeds whose main function is the storage of proteins that are used during germination for sustaining growth. PBs can also be induced to form in leaves when foreign proteins are produced at high levels in the endoplasmic reticulum (ER) and when fused to one of three tags: Zera®, elastin-like polypeptides (ELP), or hydrophobin-I (HFBI). In this study, we investigate the differences between ELP, HFBI and Zera PB formation, packing, and communication. Our results confirm the ER origin of all three fusion-tag-induced PBs. We show that secretory pathway proteins can be sequestered into all types of PBs but with different patterns, and that different fusion tags can target a specific protein to different PBs. Zera PBs are mobile and dependent on actomyosin motility similar to ELP and HFBI PBs. We show in vivo trafficking of proteins between PBs using GFP photoconversion. We also show that protein trafficking between ELP or HFBI PBs is faster and proteins travel further when compared to Zera PBs. Our results indicate that fusion-tag-induced PBs do not represent terminally stored cytosolic organelles, but that they form in, and remain part of the ER, and dynamically communicate with each other via the ER. We hypothesize that the previously documented PB mobility along the actin cytoskeleton is associated with ER movement rather than independent streaming of detached organelles. Frontiers Media S.A. 2016-05-23 /pmc/articles/PMC4876836/ /pubmed/27242885 http://dx.doi.org/10.3389/fpls.2016.00693 Text en Copyright © 2016 Saberianfar, Sattarzadeh, Joensuu, Kohalmi and Menassa. http://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) or licensor 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 Saberianfar, Reza Sattarzadeh, Amirali Joensuu, Jussi J. Kohalmi, Susanne E. Menassa, Rima Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum |
title | Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum |
title_full | Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum |
title_fullStr | Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum |
title_full_unstemmed | Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum |
title_short | Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum |
title_sort | protein bodies in leaves exchange contents through the endoplasmic reticulum |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4876836/ https://www.ncbi.nlm.nih.gov/pubmed/27242885 http://dx.doi.org/10.3389/fpls.2016.00693 |
work_keys_str_mv | AT saberianfarreza proteinbodiesinleavesexchangecontentsthroughtheendoplasmicreticulum AT sattarzadehamirali proteinbodiesinleavesexchangecontentsthroughtheendoplasmicreticulum AT joensuujussij proteinbodiesinleavesexchangecontentsthroughtheendoplasmicreticulum AT kohalmisusannee proteinbodiesinleavesexchangecontentsthroughtheendoplasmicreticulum AT menassarima proteinbodiesinleavesexchangecontentsthroughtheendoplasmicreticulum |