Protein bodies in leaves exchange contents through the endoplasmic reticulum

Reza Saberianfar, Amirali Sattarzadeh, Jussi Joonas Joensuu, Susanne E. Kohalmi, Rima Menassa

Research output: Contribution to journalArticleScientificpeer-review

10 Citations (Scopus)

Abstract

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: Zerar, 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.
Original languageEnglish
Article number693
JournalFrontiers in Plant Science
Volume7
DOIs
Publication statusPublished - 2016
MoE publication typeA1 Journal article-refereed

Fingerprint

protein bodies
endoplasmic reticulum
leaves
elastin
polypeptides
organelles
protein transport
proteins
body protein
storage proteins
microfilaments
travel

Keywords

  • confocal microscopy
  • elastin-like polypeptides (ELP)
  • hydrophobin (HFBI)
  • nicotiana benthamiana
  • protein body
  • protein body formation
  • protein trafficking
  • zera

Cite this

Saberianfar, R., Sattarzadeh, A., Joensuu, J. J., Kohalmi, S. E., & Menassa, R. (2016). Protein bodies in leaves exchange contents through the endoplasmic reticulum. Frontiers in Plant Science, 7, [693]. https://doi.org/10.3389/fpls.2016.00693
Saberianfar, Reza ; Sattarzadeh, Amirali ; Joensuu, Jussi Joonas ; Kohalmi, Susanne E. ; Menassa, Rima. / Protein bodies in leaves exchange contents through the endoplasmic reticulum. In: Frontiers in Plant Science. 2016 ; Vol. 7.
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abstract = "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: Zerar, 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.",
keywords = "confocal microscopy, elastin-like polypeptides (ELP), hydrophobin (HFBI), nicotiana benthamiana, protein body, protein body formation, protein trafficking, zera",
author = "Reza Saberianfar and Amirali Sattarzadeh and Joensuu, {Jussi Joonas} and Kohalmi, {Susanne E.} and Rima Menassa",
year = "2016",
doi = "10.3389/fpls.2016.00693",
language = "English",
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journal = "Frontiers in Plant Science",
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publisher = "Frontiers Media",

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Saberianfar, R, Sattarzadeh, A, Joensuu, JJ, Kohalmi, SE & Menassa, R 2016, 'Protein bodies in leaves exchange contents through the endoplasmic reticulum', Frontiers in Plant Science, vol. 7, 693. https://doi.org/10.3389/fpls.2016.00693

Protein bodies in leaves exchange contents through the endoplasmic reticulum. / Saberianfar, Reza; Sattarzadeh, Amirali; Joensuu, Jussi Joonas; Kohalmi, Susanne E.; Menassa, Rima.

In: Frontiers in Plant Science, Vol. 7, 693, 2016.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Protein bodies in leaves exchange contents through the endoplasmic reticulum

AU - Saberianfar, Reza

AU - Sattarzadeh, Amirali

AU - Joensuu, Jussi Joonas

AU - Kohalmi, Susanne E.

AU - Menassa, Rima

PY - 2016

Y1 - 2016

N2 - 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: Zerar, 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.

AB - 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: Zerar, 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.

KW - confocal microscopy

KW - elastin-like polypeptides (ELP)

KW - hydrophobin (HFBI)

KW - nicotiana benthamiana

KW - protein body

KW - protein body formation

KW - protein trafficking

KW - zera

U2 - 10.3389/fpls.2016.00693

DO - 10.3389/fpls.2016.00693

M3 - Article

VL - 7

JO - Frontiers in Plant Science

JF - Frontiers in Plant Science

SN - 1664-462X

M1 - 693

ER -