Abstract
Protein bodies (PBs) are endoplasmic reticulum (ER)
derived organelles originally found in seeds whose
function is to accumulate seed storage proteins. It has
been shown that PB formation is not limited to seeds and
green fluorescent protein (GFP) fused to either
elastin-like polypeptide (ELP) or hydrophobin (HFBI)
fusion tags induce the formation of PBs in leaves of N.
benthamiana. In this study, we compared the ELP- and
HFBI-induced PBs and showed that ELP-induced PBs are
larger than HFBI-induced PBs. The size of ELP- and
HFBI-induced PBs increased over time along with the
accumulation levels of their fused protein. Our results
show that PB formation is a concentration-dependent
mechanism in which proteins accumulating at levels higher
than 0.2% of total soluble protein are capable of
inducing PBs in vivo. Our results show that the presence
of fusion tags is not necessary for the formation of PBs,
but affects the distribution pattern and size of PBs.
This was confirmed by PBs induced by fluorescent proteins
as well as fungal xylanases. We noticed that in the
process of PB formation, secretory and ER-resident
molecules are passively sequestered into the lumen of
PBs. We propose to use this property of PBs as a tool to
increase the accumulation levels of erythropoietin and
human interleukin-10 by co-expression with PB-inducing
proteins.
| Original language | English |
|---|---|
| Pages (from-to) | 927-937 |
| Journal | Plant Biotechnology Journal |
| Volume | 13 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 2015 |
| MoE publication type | A1 Journal article-refereed |
Keywords
- Nicotiana benthamiana
- elastin-like polypeptides
- hydrophobin
- PB
- protein body formation
- protein body
- transient expression