UBC 18 mediates ERF 1 degradation under light–dark cycles
Summary Ethylene Response Factor 1 ( ERF 1 ) plays a crucial role in biotic and abiotic stress responses. Previous studies have shown that ERF 1 regulates stress‐responsive gene expression by binding to different cis ‐acting elements in response to various stress signals. ERF 1 was also reported to...
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Published in | The New phytologist Vol. 213; no. 3; pp. 1156 - 1167 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
01.02.2017
|
Online Access | Get full text |
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Summary: | Summary
Ethylene Response Factor 1
(
ERF
1
) plays a crucial role in biotic and abiotic stress responses. Previous studies have shown that
ERF
1
regulates stress‐responsive gene expression by binding to different
cis
‐acting elements in response to various stress signals.
ERF
1 was also reported to be unstable in the dark, and it regulates hypocotyl elongation. Here, we elucidated the mechanism underlying degradation of
ERF
1.
Yeast two‐hybrid screening showed that
UBIQUITIN
‐
CONJUGATING ENZYME
18 (
UBC
18) interacted with
ERF
1. The interaction between
ERF
1 and
UBC
18 was verified using pull‐down assays and coimmunoprecipitation analyses. We then compared the
ERF
1 protein abundance in the
UBC
18
mutant and overexpression plants. Based on the results of protein degradation and
in vivo
ubiquitination assays, we proposed that
UBC
18 mediates
ERF
1 ubiquitination and degradation.
ERF
1 was more stable in
UBC
18
mutants and less stable in
UBC
18
overexpression lines compared with that in wild‐type plants.
ERF
1 was degraded by the 26S proteasome system via regulation of
UBC
18 and promotes dark‐repression of downstream genes and proline accumulation.
UBC
18 negatively regulated drought and salt stress responses by altering the abundance of
ERF
1 and the expression of genes downstream of
ERF
1. |
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ISSN: | 0028-646X 1469-8137 |
DOI: | 10.1111/nph.14272 |