scholarly journals Roles of pepper bZIP protein CaDILZ1 and its interacting partner RING-type E3 ligase CaDSR1 in modulation of drought tolerance

2018 ◽  
Vol 96 (2) ◽  
pp. 452-467 ◽  
Author(s):  
Chae Woo Lim ◽  
Woonhee Baek ◽  
Sung Chul Lee
Keyword(s):  
Drought Tolerance ◽  
E3 Ligase ◽  
Bzip Protein ◽  
Ring Type

Zinc-finger protein MdBBX7/MdCOL9, a target of MdMIEL1 E3 ligase, confers drought tolerance in apple

2021 ◽  
Author(s):  
Pengxiang Chen ◽  
Fang Zhi ◽  
Xuewei Li ◽  
Wenyun Shen ◽  
Mingjia Yan ◽  
...  
Keyword(s):  
Drought Stress ◽  
Drought Tolerance ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
E3 Ligase ◽  
26S Proteasome ◽  
Negative Regulator ◽  
Binding Motif ◽  
Ethylene Response Factor ◽  
Finger Protein

Abstract Water deficit is one of the main challenges for apple (Malus × domestica) growth and productivity. Breeding drought-tolerant cultivars depends on a thorough understanding of the drought responses of apple trees. Here, we identified the zinc-finger protein B-BOX 7/CONSTANS-LIKE 9 (MdBBX7/MdCOL9), which plays a positive role in apple drought tolerance. The overexpression of MdBBX7 enhanced drought tolerance, whereas knocking down MdBBX7 expression reduced it. Chromatin immunoprecipitation-sequencing (ChIP-seq) analysis identified one cis-element of MdBBX7, CCTTG, as well as its known binding motif, the T/G box. ChIP-seq and RNA-seq identified 1,197 direct targets of MdBBX7, including ETHYLENE RESPONSE FACTOR (ERF1), EARLY RESPONSIVE TO DEHYDRATION 15 (ERD15), and GOLDEN2-LIKE 1 (GLK1) and these were further verified by ChIP-qPCR and electronic mobility shift assays. Yeast two-hybrid screen identified an interacting protein of MdBBX7, RING-type E3 ligase MYB30-INTERACTING E3 LIGASE 1 (MIEL1). Further examination revealed that MdMIEL1 could mediate the ubiquitination and degradation of MdBBX7 by the 26S proteasome pathway. Genetic interaction analysis suggested that MdMIEL1 acts as an upstream factor of MdBBX7. In addition, MdMIEL1 was a negative regulator of the apple drought stress response. Taken together, our results illustrate the molecular mechanisms by which the MdMIEL1–MdBBX7 module influences the response of apple to drought stress.

The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type

2004 ◽  
Vol 11 (10) ◽  
pp. 984-991 ◽  
Author(s):  
Andrea Pichler ◽  
Puck Knipscheer ◽  
Hisato Saitoh ◽  
Titia K Sixma ◽  
Frauke Melchior
Keyword(s):  
E3 Ligase ◽  
Ring Type ◽  
Sumo E3 Ligase

scholarly journals An Arabidopsis E3 ligase HUB2 increases histone H2B monoubiquitination and enhances drought tolerance in transgenic cotton

2018 ◽  
Vol 17 (3) ◽  
pp. 556-568 ◽  
Author(s):  
Hong Chen ◽  
Hao Feng ◽  
Xueyan Zhang ◽  
Chaojun Zhang ◽  
Tao Wang ◽  
...  
Keyword(s):  
Drought Tolerance ◽  
E3 Ligase ◽  
Transgenic Cotton ◽  
Histone H2b

scholarly journals A RING-type E3 ligase controls anther dehiscence by activating the jasmonate biosynthetic pathway geneDEFECTIVE IN ANTHER DEHISCENCE1in Arabidopsis

2013 ◽  
Vol 74 (2) ◽  
pp. 310-327 ◽  
Author(s):  
Yan-Jhu Peng ◽  
Ching-Fang Shih ◽  
Jun-Yi Yang ◽  
Choon-Meng Tan ◽  
Wei-Han Hsu ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
E3 Ligase ◽  
Anther Dehiscence ◽  
Ring Type

scholarly journals The ARRE RING-Type E3 Ubiquitin Ligase Negatively Regulates Cuticular Wax Biosynthesis in Arabidopsis thaliana by Controlling ECERIFERUM1 and ECERIFERUM3 Protein Levels

2021 ◽  
Vol 12 ◽  
Author(s):  
Shuang Liu ◽  
Meixuezi Tong ◽  
Lifang Zhao ◽  
Xin Li ◽  
Ljerka Kunst
Keyword(s):  
Ubiquitin Ligase ◽  
Uv Light ◽  
E3 Ubiquitin Ligase ◽  
E3 Ligase ◽  
Cuticular Wax ◽  
26S Proteasome ◽  
Covalent Attachment ◽  
Wax Deposition ◽  
E3 Ligases ◽  
Ring Type

The outer epidermal cell walls of plant shoots are covered with a cuticle, a continuous lipid structure that provides protection from desiccation, UV light, pathogens, and insects. The cuticle is mostly composed of cutin and cuticular wax. Cuticular wax synthesis is synchronized with surface area expansion during plant development and is associated with plant responses to biotic and abiotic stresses. Cuticular wax deposition is tightly regulated by well-established transcriptional and post-transcriptional regulatory mechanisms, as well as post-translationally via the ubiquitin-26S proteasome system (UPS). The UPS is highly conserved in eukaryotes and involves the covalent attachment of polyubiquitin chains to the target protein by an E3 ligase, followed by the degradation of the modified protein by the 26S proteasome. A large number of E3 ligases are encoded in the Arabidopsis genome, but only a few have been implicated in the regulation of cuticular wax deposition. In this study, we have conducted an E3 ligase reverse genetic screen and identified a novel RING-type E3 ubiquitin ligase, AtARRE, which negatively regulates wax biosynthesis in Arabidopsis. Arabidopsis plants overexpressing AtARRE exhibit glossy stems and siliques, reduced fertility and fusion between aerial organs. Wax load and wax compositional analyses of AtARRE overexpressors showed that the alkane-forming branch of the wax biosynthetic pathway is affected. Co-expression of AtARRE and candidate target proteins involved in alkane formation in both Nicotiana benthamiana and stable Arabidopsis transgenic lines demonstrated that AtARRE controls the levels of wax biosynthetic enzymes ECERIFERUM1 (CER1) and ECERIFERUM3 (CER3). CER1 has also been confirmed to be a ubiquitination substrate of the AtARRE E3 ligase by an in vivo ubiquitination assay using a reconstituted Escherichia coli system. The AtARRE gene is expressed throughout the plant, with the highest expression detected in fully expanded rosette leaves and oldest stem internodes. AtARRE gene expression can also be induced by exposure to pathogens. These findings reveal that wax biosynthesis in mature plant tissues and in response to pathogen infection is controlled post-translationally.

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