PUB22 and PUB23 U-BOX E3 ligases directly ubiquitinate RPN6, a 26S proteasome lid subunit, for subsequent degradation in Arabidopsis thaliana

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PUB22 and PUB23 U-BOX E3 ligases directly ubiquitinate RPN6, a 26S proteasome lid subunit, for subsequent degradation in Arabidopsis thaliana. / Cho, Seok Keun; Bae, Hansol; Ryu, Moonyoung; Yang, Seong Wook; Kim, Woo Taek.

In: Biochemical and Biophysical Research Communications, Vol. 464, No. 4, 2015, p. 994-999.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Cho, SK, Bae, H, Ryu, M, Yang, SW & Kim, WT 2015, 'PUB22 and PUB23 U-BOX E3 ligases directly ubiquitinate RPN6, a 26S proteasome lid subunit, for subsequent degradation in Arabidopsis thaliana', Biochemical and Biophysical Research Communications, vol. 464, no. 4, pp. 994-999. https://doi.org/10.1016/j.bbrc.2015.07.030

APA

Cho, S. K., Bae, H., Ryu, M., Yang, S. W., & Kim, W. T. (2015). PUB22 and PUB23 U-BOX E3 ligases directly ubiquitinate RPN6, a 26S proteasome lid subunit, for subsequent degradation in Arabidopsis thaliana. Biochemical and Biophysical Research Communications, 464(4), 994-999. https://doi.org/10.1016/j.bbrc.2015.07.030

Vancouver

Cho SK, Bae H, Ryu M, Yang SW, Kim WT. PUB22 and PUB23 U-BOX E3 ligases directly ubiquitinate RPN6, a 26S proteasome lid subunit, for subsequent degradation in Arabidopsis thaliana. Biochemical and Biophysical Research Communications. 2015;464(4):994-999. https://doi.org/10.1016/j.bbrc.2015.07.030

Author

Cho, Seok Keun ; Bae, Hansol ; Ryu, Moonyoung ; Yang, Seong Wook ; Kim, Woo Taek. / PUB22 and PUB23 U-BOX E3 ligases directly ubiquitinate RPN6, a 26S proteasome lid subunit, for subsequent degradation in Arabidopsis thaliana. In: Biochemical and Biophysical Research Communications. 2015 ; Vol. 464, No. 4. pp. 994-999.

Bibtex

@article{277dea6db6774e338086b7e8bcf35882,
title = "PUB22 and PUB23 U-BOX E3 ligases directly ubiquitinate RPN6, a 26S proteasome lid subunit, for subsequent degradation in Arabidopsis thaliana",
abstract = "Drought stress strongly affects plant growth and development, directly connected with crop yields, accordingly. However, related to the function of U-BOX E3 ligases, the underlying molecular mechanisms of desiccation stress response in plants are still largely unknown. Here we report that PUB22 and PUB23, two U-box E3 ligase homologs, tether ubiquitins to 19S proteasome regulatory particle (RP) subunit RPN6, leading to its degradation. RPN6 was identified as an interacting substrate of PUB22 by yeast two-hybrid screening, and in vitro pull-down assay confirmed that RPN6 interacts not only with PUB22, but also with PUB23. Both PUB22 and PUB23 were able to conjugate ubiquitins on RPN6 in vitro. Furthermore, RPN6 showed a shorter protein half-life in PUB22 overexpressing plants than in wild-type, besides RPN6 was significantly stabilized in pub22pub23 double knockout plants. Taken together, these results solidify a notion that PUB22 and PUB23 can alter the activity of 26S proteasome in response to drought stress.",
keywords = "26S proteasome lid complex, Drought stress, RPN6, U-BOX E3 ligase, Ubiquitin-proteasome system",
author = "Cho, {Seok Keun} and Hansol Bae and Moonyoung Ryu and Yang, {Seong Wook} and Kim, {Woo Taek}",
year = "2015",
doi = "10.1016/j.bbrc.2015.07.030",
language = "English",
volume = "464",
pages = "994--999",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - PUB22 and PUB23 U-BOX E3 ligases directly ubiquitinate RPN6, a 26S proteasome lid subunit, for subsequent degradation in Arabidopsis thaliana

AU - Cho, Seok Keun

AU - Bae, Hansol

AU - Ryu, Moonyoung

AU - Yang, Seong Wook

AU - Kim, Woo Taek

PY - 2015

Y1 - 2015

N2 - Drought stress strongly affects plant growth and development, directly connected with crop yields, accordingly. However, related to the function of U-BOX E3 ligases, the underlying molecular mechanisms of desiccation stress response in plants are still largely unknown. Here we report that PUB22 and PUB23, two U-box E3 ligase homologs, tether ubiquitins to 19S proteasome regulatory particle (RP) subunit RPN6, leading to its degradation. RPN6 was identified as an interacting substrate of PUB22 by yeast two-hybrid screening, and in vitro pull-down assay confirmed that RPN6 interacts not only with PUB22, but also with PUB23. Both PUB22 and PUB23 were able to conjugate ubiquitins on RPN6 in vitro. Furthermore, RPN6 showed a shorter protein half-life in PUB22 overexpressing plants than in wild-type, besides RPN6 was significantly stabilized in pub22pub23 double knockout plants. Taken together, these results solidify a notion that PUB22 and PUB23 can alter the activity of 26S proteasome in response to drought stress.

AB - Drought stress strongly affects plant growth and development, directly connected with crop yields, accordingly. However, related to the function of U-BOX E3 ligases, the underlying molecular mechanisms of desiccation stress response in plants are still largely unknown. Here we report that PUB22 and PUB23, two U-box E3 ligase homologs, tether ubiquitins to 19S proteasome regulatory particle (RP) subunit RPN6, leading to its degradation. RPN6 was identified as an interacting substrate of PUB22 by yeast two-hybrid screening, and in vitro pull-down assay confirmed that RPN6 interacts not only with PUB22, but also with PUB23. Both PUB22 and PUB23 were able to conjugate ubiquitins on RPN6 in vitro. Furthermore, RPN6 showed a shorter protein half-life in PUB22 overexpressing plants than in wild-type, besides RPN6 was significantly stabilized in pub22pub23 double knockout plants. Taken together, these results solidify a notion that PUB22 and PUB23 can alter the activity of 26S proteasome in response to drought stress.

KW - 26S proteasome lid complex

KW - Drought stress

KW - RPN6

KW - U-BOX E3 ligase

KW - Ubiquitin-proteasome system

U2 - 10.1016/j.bbrc.2015.07.030

DO - 10.1016/j.bbrc.2015.07.030

M3 - Journal article

C2 - 26188517

AN - SCOPUS:84940459541

VL - 464

SP - 994

EP - 999

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -

ID: 156414565