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중앙대학교

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Plant Cell Environ., Jan 14 2024, | https://doi.org/10.1111/pce.14818 A pepper RING-finger E3 ligase, CaFIRF1, negatively regulates the high-salt stress response by modulating the stability of CaFAF1

Yeongil Bae, Woonhee Baek, Chae Woo Lim, Sung Chul Lee

Department of Life Science (BK21 Program),Chung‐Ang University, Seoul, Korea

Yeongil Bae and Woonhee Baek contributed equally to this work.

Correspondence Chae Woo Lim and Sung Chul Lee

Abstract

Controlling protein stability or degradation via the ubiquitin-26S proteasome system is a crucial mechanism in plant cellular responses to stress conditions. Previous studies have revealed that the pepper FANTASTIC FOUR-like gene, CaFAF1, plays a positive role in salt tolerance and that, in this process, CaFAF1 protein degradation is delayed. Here, we sought to isolate the E3 ligases potentially responsible for modulating CaFAF1 protein stability in response to salt stress. The pepper RING-type E3 ligase CaFIRF1 (Capsicum annuum FAF1 Interacting RING Finger protein 1) was found to interact with and ubiquitinate CaFAF1, leading to the degradation of CaFAF1 proteins. In response to high-salt treatments, CaFIRF1-silenced pepper plants exhibited tolerant phenotypes. In contrast, co-silencing of CaFAF1 and CaFIRF1 led to increased sensitivity to high-salt treatments, revealing that CaFIRF1 functions upstream of CaFAF1. A cell-free degradation analysis showed that high-salt treatment suppressed CaFAF1 protein degradation via the 26S proteasome pathway, in which CaFIRF1 is functionally involved. In addition, an in vivo ubiquitination assay revealed that CaFIRF1-mediated ubiquitination of CaFAF1 proteins was reduced by high-salt treatment. Taken together, these findings suggest that the degradation of CaFAF1 mediated by CaFIRF1 has a critical role in pepper plant responses to high salinity.

논문정보

형식Research article
게재일2024년 01월 (BRIC 등록일 2024-01-16)
연구진국내 연구진
분야 생명과학 > 식물학

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