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...

Descripción completa

Detalles Bibliográficos
Autores principales: Saberianfar, Reza, Sattarzadeh, Amirali, Joensuu, Jussi J., Kohalmi, Susanne E., Menassa, Rima
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