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Sequence-specific protein aggregation generates defined protein knockdowns in plants

Camilla Betti, Isabelle Vanhoutte UGent, Silvie Coutuer UGent, Riet De Rycke UGent, Kiril Mishev, Marnik Vuylsteke UGent, Stijn Aesaert UGent, Debbie Rombaut UGent, Rodrigo Gallardo, Frederik De Smet, et al. (2016) PLANT PHYSIOLOGY. 171(2). p.773-787
abstract
Protein aggregation is determined by short (5-15 amino acids) aggregation-prone regions (APRs) of the polypeptide sequence that self-associate in a specific manner to form beta-structured inclusions. Here, we demonstrate that the sequence specificity of APRs can be exploited to selectively knock down proteins with different localization and function in plants. Synthetic aggregation-prone peptides derived from the APRs of either the negative regulators of the brassinosteroid (BR) signaling, the glycogen synthase kinase 3/Arabidopsis SHAGGY-like kinases (GSK3/ASKs), or the starch-degrading enzyme alpha-glucan water dikinase were designed. Stable expression of the APRs in Arabidopsis (Arabidopsis thaliana) and maize (Zea mays) induced aggregation of the target proteins, giving rise to plants displaying constitutive BR responses and increased starch content, respectively. Overall, we show that the sequence specificity of APRs can be harnessed to generate aggregation-associated phenotypes in a targeted manner in different subcellular compartments. This study points toward the potential application of induced targeted aggregation as a useful tool to knock down protein functions in plants and, especially, to generate beneficial traits in crops.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
BUILDING-BLOCKS, MAIZE, ARABIDOPSIS, TRANSGENIC PLANTS, GSK3-LIKE KINASES, BRASSINOSTEROID BIOSYNTHESIS, CELL-DIVISION, AMYLOID-LIKE FIBRILS, GENE, GROWTH
journal title
PLANT PHYSIOLOGY
Plant Physiol.
volume
171
issue
2
pages
773 - 787
Web of Science type
Article
Web of Science id
000380699200004
JCR category
PLANT SCIENCES
JCR impact factor
6.456 (2016)
JCR rank
11/211 (2016)
JCR quartile
1 (2016)
ISSN
0032-0889
DOI
10.1104/pp.16.00335
project
Biotechnology for a sustainable economy (Bio-Economy)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have retained and own the full copyright for this publication
id
8112936
handle
http://hdl.handle.net/1854/LU-8112936
date created
2016-10-13 09:29:14
date last changed
2017-07-03 10:31:29
@article{8112936,
  abstract     = {Protein aggregation is determined by short (5-15 amino acids) aggregation-prone regions (APRs) of the polypeptide sequence that self-associate in a specific manner to form beta-structured inclusions. Here, we demonstrate that the sequence specificity of APRs can be exploited to selectively knock down proteins with different localization and function in plants. Synthetic aggregation-prone peptides derived from the APRs of either the negative regulators of the brassinosteroid (BR) signaling, the glycogen synthase kinase 3/Arabidopsis SHAGGY-like kinases (GSK3/ASKs), or the starch-degrading enzyme alpha-glucan water dikinase were designed. Stable expression of the APRs in Arabidopsis (Arabidopsis thaliana) and maize (Zea mays) induced aggregation of the target proteins, giving rise to plants displaying constitutive BR responses and increased starch content, respectively. Overall, we show that the sequence specificity of APRs can be harnessed to generate aggregation-associated phenotypes in a targeted manner in different subcellular compartments. This study points toward the potential application of induced targeted aggregation as a useful tool to knock down protein functions in plants and, especially, to generate beneficial traits in crops.},
  author       = {Betti, Camilla and Vanhoutte, Isabelle and Coutuer, Silvie and De Rycke, Riet and Mishev, Kiril and Vuylsteke, Marnik and Aesaert, Stijn and Rombaut, Debbie and Gallardo, Rodrigo and De Smet, Frederik and Xu, Jie and Van Lijsebettens, Maria and Van Breusegem, Frank and Inz{\'e}, Dirk and Rousseau, Frederic and Schymkowitz, Joost and Russinova, Eugenia},
  issn         = {0032-0889},
  journal      = {PLANT PHYSIOLOGY},
  keyword      = {BUILDING-BLOCKS,MAIZE,ARABIDOPSIS,TRANSGENIC PLANTS,GSK3-LIKE KINASES,BRASSINOSTEROID BIOSYNTHESIS,CELL-DIVISION,AMYLOID-LIKE FIBRILS,GENE,GROWTH},
  language     = {eng},
  number       = {2},
  pages        = {773--787},
  title        = {Sequence-specific protein aggregation generates defined protein knockdowns in plants},
  url          = {http://dx.doi.org/10.1104/pp.16.00335},
  volume       = {171},
  year         = {2016},
}

Chicago
Betti, Camilla, Isabelle Vanhoutte, Silvie Coutuer, Riet De Rycke, Kiril Mishev, Marnik Vuylsteke, Stijn Aesaert, et al. 2016. “Sequence-specific Protein Aggregation Generates Defined Protein Knockdowns in Plants.” Plant Physiology 171 (2): 773–787.
APA
Betti, C., Vanhoutte, I., Coutuer, S., De Rycke, R., Mishev, K., Vuylsteke, M., Aesaert, S., et al. (2016). Sequence-specific protein aggregation generates defined protein knockdowns in plants. PLANT PHYSIOLOGY, 171(2), 773–787.
Vancouver
1.
Betti C, Vanhoutte I, Coutuer S, De Rycke R, Mishev K, Vuylsteke M, et al. Sequence-specific protein aggregation generates defined protein knockdowns in plants. PLANT PHYSIOLOGY. 2016;171(2):773–87.
MLA
Betti, Camilla, Isabelle Vanhoutte, Silvie Coutuer, et al. “Sequence-specific Protein Aggregation Generates Defined Protein Knockdowns in Plants.” PLANT PHYSIOLOGY 171.2 (2016): 773–787. Print.