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Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum

Journal Article · · Frontiers in Plant Science
 [1];  [2];  [3];  [4];  [5]
  1. Argiculture and Agri-Food Canada, London, ON (Canada); Univ. of Western Ontario, London, ON (Canada). Dept. of Biology; VVT Technical Research Centre of Finland
  2. Cornell Univ., Ithaca, NY (United States). Dept. of Molecular Biology and Genetics
  3. VTT Technical Research Centre of Finland, Espoo (Finland)
  4. Univ. of Western Ontario, London, ON (Canada). Dept. of Biology
  5. Argiculture and Agri-Food Canada, London, ON (Canada); Univ. of Western Ontario, London, ON (Canada). Dept. of Biology
+ Show Author Affiliations
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). Here 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.
Research Organization:
Argiculture and Agri-Food Canada, London, ON (Canada); Cornell Univ., Ithaca, NY (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Grant/Contract Number:
SC0002628
OSTI ID:
1393394
Journal Information:
Frontiers in Plant Science, Journal Name: Frontiers in Plant Science Vol. 7; ISSN 1664-462X
Publisher:
Frontiers Research FoundationCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (5)

Recognition motifs rather than phylogenetic origin influence the ability of targeting peptides to import nuclear-encoded recombinant proteins into rice mitochondria journal October 2019
Dynamics of liquid-liquid phase separation of wheat gliadins journal September 2018
LALF32-51 -E7, a HPV-16 therapeutic vaccine candidate, forms protein body-like structures when expressed in Nicotiana benthamiana leaves journal September 2017
Transient Expression of Dengue Virus NS1 Antigen in Nicotiana benthamiana for Use as a Diagnostic Antigen journal January 2020
Russell-Like Bodies in Plant Seeds Share Common Features With Prolamin Bodies and Occur Upon Recombinant Protein Production journal June 2019

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Nicotiana benthamiana
confocal microscopy
elastin-like polypeptides (ELP)
hydrophobin (HFBI)
protein body
protein body formation
protein trafficking
zera