E3 SUMO ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development

Sung Il Kim, Bongsoo Park, Do Youn Kim, Song Yion Yeu, Sang Ik Song, Jong Tae Song, Hak Soo Seo

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Gibberellins affect various plant development processes including germination, cell division and elongation, and flowering. A large number of studies have been carried out to address the molecular mechanisms that mediate gibberellin signalling effects on plant growth. However, such studies have been limited to DELLA protein degradation; the regulatory mechanisms controlling how the stability and function of SLEEPY1 (SLY1), a protein that interacts with target DELLA proteins as components of the Skp, Cullin, F-box (SCF)SLY1 complex, are modulated at the post-translational level have not been addressed. In the present study, we show that the E3 SUMO (small ubiquitin-related modifier) ligase AtSIZ1 regulates gibberellic acid signalling in Arabidopsis species by sumoylating SLY1. SLY1 was less abundant in siz1-2 mutants than in wild-type plants, but the DELLA protein repressor of ga1-3 (RGA) was more abundant in siz1-2 mutants than in wild-type plants. SLY1 also accumulated to a high level in the SUMO protease mutant esd4. Transgenic sly1-13 mutants over-expressing SLY1 were phenotypically similar to wild-type plants; however, sly1-13 plants over-expressing a mutated mSLY1 protein (K122R, a mutation at the sumoylation site) retained the mutant dwarfing phenotype. Over-expression of SLY1 in sly1-13 mutants resulted in a return of RGA levels to wild-type levels, but RGA accumulated to high levels in mutants overexpressing mSLY1. RGA was clearly detected in Arabidopsis co-expressing AtSIZ1 and mSLY1, but not in plants co-expressing AtSIZ1 and SLY1. In addition, sumoylated SLY1 interacted with RGA and SLY1 sumoylation was significantly increased by GA. Taken together, our results indicate that, in Arabidopsis, AtSIZ1 positively controls GA signalling through SLY1 sumoylation.

Original languageEnglish (US)
Pages (from-to)299-314
Number of pages16
JournalBiochemical Journal
Volume469
Issue number2
DOIs
StatePublished - Jul 15 2015

Fingerprint

Plant Development
Ligases
Ubiquitin
Sumoylation
Gibberellins
Arabidopsis
Proteins
Cullin Proteins
Plant Proteins
Elongation
Germination
Peptide Hydrolases
Cell Division
Cells
Proteolysis
Degradation
Phenotype
Mutation
Growth

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Kim, S. I., Park, B., Kim, D. Y., Yeu, S. Y., Song, S. I., Song, J. T., & Seo, H. S. (2015). E3 SUMO ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development. Biochemical Journal, 469(2), 299-314. https://doi.org/10.1042/BJ20141302
Kim, Sung Il ; Park, Bongsoo ; Kim, Do Youn ; Yeu, Song Yion ; Song, Sang Ik ; Song, Jong Tae ; Seo, Hak Soo. / E3 SUMO ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development. In: Biochemical Journal. 2015 ; Vol. 469, No. 2. pp. 299-314.
@article{9818dc887c704ef6a35e93840206339a,
title = "E3 SUMO ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development",
abstract = "Gibberellins affect various plant development processes including germination, cell division and elongation, and flowering. A large number of studies have been carried out to address the molecular mechanisms that mediate gibberellin signalling effects on plant growth. However, such studies have been limited to DELLA protein degradation; the regulatory mechanisms controlling how the stability and function of SLEEPY1 (SLY1), a protein that interacts with target DELLA proteins as components of the Skp, Cullin, F-box (SCF)SLY1 complex, are modulated at the post-translational level have not been addressed. In the present study, we show that the E3 SUMO (small ubiquitin-related modifier) ligase AtSIZ1 regulates gibberellic acid signalling in Arabidopsis species by sumoylating SLY1. SLY1 was less abundant in siz1-2 mutants than in wild-type plants, but the DELLA protein repressor of ga1-3 (RGA) was more abundant in siz1-2 mutants than in wild-type plants. SLY1 also accumulated to a high level in the SUMO protease mutant esd4. Transgenic sly1-13 mutants over-expressing SLY1 were phenotypically similar to wild-type plants; however, sly1-13 plants over-expressing a mutated mSLY1 protein (K122R, a mutation at the sumoylation site) retained the mutant dwarfing phenotype. Over-expression of SLY1 in sly1-13 mutants resulted in a return of RGA levels to wild-type levels, but RGA accumulated to high levels in mutants overexpressing mSLY1. RGA was clearly detected in Arabidopsis co-expressing AtSIZ1 and mSLY1, but not in plants co-expressing AtSIZ1 and SLY1. In addition, sumoylated SLY1 interacted with RGA and SLY1 sumoylation was significantly increased by GA. Taken together, our results indicate that, in Arabidopsis, AtSIZ1 positively controls GA signalling through SLY1 sumoylation.",
author = "Kim, {Sung Il} and Bongsoo Park and Kim, {Do Youn} and Yeu, {Song Yion} and Song, {Sang Ik} and Song, {Jong Tae} and Seo, {Hak Soo}",
year = "2015",
month = "7",
day = "15",
doi = "10.1042/BJ20141302",
language = "English (US)",
volume = "469",
pages = "299--314",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "2",

}

Kim, SI, Park, B, Kim, DY, Yeu, SY, Song, SI, Song, JT & Seo, HS 2015, 'E3 SUMO ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development', Biochemical Journal, vol. 469, no. 2, pp. 299-314. https://doi.org/10.1042/BJ20141302

E3 SUMO ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development. / Kim, Sung Il; Park, Bongsoo; Kim, Do Youn; Yeu, Song Yion; Song, Sang Ik; Song, Jong Tae; Seo, Hak Soo.

In: Biochemical Journal, Vol. 469, No. 2, 15.07.2015, p. 299-314.

Research output: Contribution to journalArticle

TY - JOUR

T1 - E3 SUMO ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development

AU - Kim, Sung Il

AU - Park, Bongsoo

AU - Kim, Do Youn

AU - Yeu, Song Yion

AU - Song, Sang Ik

AU - Song, Jong Tae

AU - Seo, Hak Soo

PY - 2015/7/15

Y1 - 2015/7/15

N2 - Gibberellins affect various plant development processes including germination, cell division and elongation, and flowering. A large number of studies have been carried out to address the molecular mechanisms that mediate gibberellin signalling effects on plant growth. However, such studies have been limited to DELLA protein degradation; the regulatory mechanisms controlling how the stability and function of SLEEPY1 (SLY1), a protein that interacts with target DELLA proteins as components of the Skp, Cullin, F-box (SCF)SLY1 complex, are modulated at the post-translational level have not been addressed. In the present study, we show that the E3 SUMO (small ubiquitin-related modifier) ligase AtSIZ1 regulates gibberellic acid signalling in Arabidopsis species by sumoylating SLY1. SLY1 was less abundant in siz1-2 mutants than in wild-type plants, but the DELLA protein repressor of ga1-3 (RGA) was more abundant in siz1-2 mutants than in wild-type plants. SLY1 also accumulated to a high level in the SUMO protease mutant esd4. Transgenic sly1-13 mutants over-expressing SLY1 were phenotypically similar to wild-type plants; however, sly1-13 plants over-expressing a mutated mSLY1 protein (K122R, a mutation at the sumoylation site) retained the mutant dwarfing phenotype. Over-expression of SLY1 in sly1-13 mutants resulted in a return of RGA levels to wild-type levels, but RGA accumulated to high levels in mutants overexpressing mSLY1. RGA was clearly detected in Arabidopsis co-expressing AtSIZ1 and mSLY1, but not in plants co-expressing AtSIZ1 and SLY1. In addition, sumoylated SLY1 interacted with RGA and SLY1 sumoylation was significantly increased by GA. Taken together, our results indicate that, in Arabidopsis, AtSIZ1 positively controls GA signalling through SLY1 sumoylation.

AB - Gibberellins affect various plant development processes including germination, cell division and elongation, and flowering. A large number of studies have been carried out to address the molecular mechanisms that mediate gibberellin signalling effects on plant growth. However, such studies have been limited to DELLA protein degradation; the regulatory mechanisms controlling how the stability and function of SLEEPY1 (SLY1), a protein that interacts with target DELLA proteins as components of the Skp, Cullin, F-box (SCF)SLY1 complex, are modulated at the post-translational level have not been addressed. In the present study, we show that the E3 SUMO (small ubiquitin-related modifier) ligase AtSIZ1 regulates gibberellic acid signalling in Arabidopsis species by sumoylating SLY1. SLY1 was less abundant in siz1-2 mutants than in wild-type plants, but the DELLA protein repressor of ga1-3 (RGA) was more abundant in siz1-2 mutants than in wild-type plants. SLY1 also accumulated to a high level in the SUMO protease mutant esd4. Transgenic sly1-13 mutants over-expressing SLY1 were phenotypically similar to wild-type plants; however, sly1-13 plants over-expressing a mutated mSLY1 protein (K122R, a mutation at the sumoylation site) retained the mutant dwarfing phenotype. Over-expression of SLY1 in sly1-13 mutants resulted in a return of RGA levels to wild-type levels, but RGA accumulated to high levels in mutants overexpressing mSLY1. RGA was clearly detected in Arabidopsis co-expressing AtSIZ1 and mSLY1, but not in plants co-expressing AtSIZ1 and SLY1. In addition, sumoylated SLY1 interacted with RGA and SLY1 sumoylation was significantly increased by GA. Taken together, our results indicate that, in Arabidopsis, AtSIZ1 positively controls GA signalling through SLY1 sumoylation.

UR - http://www.scopus.com/inward/record.url?scp=84937151048&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84937151048&partnerID=8YFLogxK

U2 - 10.1042/BJ20141302

DO - 10.1042/BJ20141302

M3 - Article

VL - 469

SP - 299

EP - 314

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -