Ubiquitination of LHY by SINAT5 regulates flowering time and is inhibited by DET1

Bong Soo Park; Hee Jeong Eo; In Cheol Jang; Hong Gu Kang; Jong Tae Song; H. S. Seo Hak Soo

doi:10.1016/j.bbrc.2010.06.067

Ubiquitination of LHY by SINAT5 regulates flowering time and is inhibited by DET1

Bong Soo Park, Hee Jeong Eo, In Cheol Jang, Hong Gu Kang, Jong Tae Song, H. S. Seo Hak Soo

Research output: Contribution to journal › Article › peer-review

27 Scopus citations

Abstract

Ubiquitin is a small polypeptide and ubiquitination is the post-translational modification by ubiquitin protein, resulting in degradation of target proteins by the 26S proteasome complex. Here, we found that E3 ubiquitin ligase SINAT5, an Arabidopsis homologue of the Drosophila SINA RING-finger protein, interacts directly with LHY, a component of the circadian oscillator, and DET1, a negative regulator of light-regulated gene expression. We also found that SINAT5 has E3 ubiquitination activity for LHY but not for DET1. Interestingly, LHY ubiquitination by SINAT5 was inhibited by DET1. Late flowering of sinat5 mutants indicates that flowering time can be controlled by DET1 through regulation of LHY stability by SINAT5.

Original language	English (US)
Pages (from-to)	242-246
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	398
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2010.06.067
State	Published - Jul 2010
Externally published	Yes

Keywords

DET1
E3 ubiquitin ligase
Flowering
Interaction
LHY
SINAT5
Ubiquitin

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2010.06.067

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title = "Ubiquitination of LHY by SINAT5 regulates flowering time and is inhibited by DET1",

abstract = "Ubiquitin is a small polypeptide and ubiquitination is the post-translational modification by ubiquitin protein, resulting in degradation of target proteins by the 26S proteasome complex. Here, we found that E3 ubiquitin ligase SINAT5, an Arabidopsis homologue of the Drosophila SINA RING-finger protein, interacts directly with LHY, a component of the circadian oscillator, and DET1, a negative regulator of light-regulated gene expression. We also found that SINAT5 has E3 ubiquitination activity for LHY but not for DET1. Interestingly, LHY ubiquitination by SINAT5 was inhibited by DET1. Late flowering of sinat5 mutants indicates that flowering time can be controlled by DET1 through regulation of LHY stability by SINAT5.",

keywords = "DET1, E3 ubiquitin ligase, Flowering, Interaction, LHY, SINAT5, Ubiquitin",

author = "Park, {Bong Soo} and Eo, {Hee Jeong} and Jang, {In Cheol} and Kang, {Hong Gu} and Song, {Jong Tae} and {Seo Hak Soo}, {H. S.}",

note = "Funding Information: This work was supported by National Research Foundation of Korea Grant funded by the Korean Government (No. 2009-0070816 ) and (No. F00003 ).",

year = "2010",

month = jul,

doi = "10.1016/j.bbrc.2010.06.067",

language = "English (US)",

volume = "398",

pages = "242--246",

journal = "Biochemical and Biophysical Research Communications",

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T1 - Ubiquitination of LHY by SINAT5 regulates flowering time and is inhibited by DET1

AU - Park, Bong Soo

AU - Eo, Hee Jeong

AU - Jang, In Cheol

AU - Kang, Hong Gu

AU - Song, Jong Tae

AU - Seo Hak Soo, H. S.

N1 - Funding Information: This work was supported by National Research Foundation of Korea Grant funded by the Korean Government (No. 2009-0070816 ) and (No. F00003 ).

PY - 2010/7

Y1 - 2010/7

N2 - Ubiquitin is a small polypeptide and ubiquitination is the post-translational modification by ubiquitin protein, resulting in degradation of target proteins by the 26S proteasome complex. Here, we found that E3 ubiquitin ligase SINAT5, an Arabidopsis homologue of the Drosophila SINA RING-finger protein, interacts directly with LHY, a component of the circadian oscillator, and DET1, a negative regulator of light-regulated gene expression. We also found that SINAT5 has E3 ubiquitination activity for LHY but not for DET1. Interestingly, LHY ubiquitination by SINAT5 was inhibited by DET1. Late flowering of sinat5 mutants indicates that flowering time can be controlled by DET1 through regulation of LHY stability by SINAT5.

AB - Ubiquitin is a small polypeptide and ubiquitination is the post-translational modification by ubiquitin protein, resulting in degradation of target proteins by the 26S proteasome complex. Here, we found that E3 ubiquitin ligase SINAT5, an Arabidopsis homologue of the Drosophila SINA RING-finger protein, interacts directly with LHY, a component of the circadian oscillator, and DET1, a negative regulator of light-regulated gene expression. We also found that SINAT5 has E3 ubiquitination activity for LHY but not for DET1. Interestingly, LHY ubiquitination by SINAT5 was inhibited by DET1. Late flowering of sinat5 mutants indicates that flowering time can be controlled by DET1 through regulation of LHY stability by SINAT5.

KW - DET1

KW - E3 ubiquitin ligase

KW - Flowering

KW - Interaction

KW - LHY

KW - SINAT5

KW - Ubiquitin

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Ubiquitination of LHY by SINAT5 regulates flowering time and is inhibited by DET1

Abstract

Keywords

ASJC Scopus subject areas

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