scholarly journals A RING-Type E3 Ubiquitin Ligase, OsGW2, Controls Chlorophyll Content and Dark-Induced Senescence in Rice

2020 ◽  
Vol 21 (5) ◽  
pp. 1704 ◽  
Author(s):  
Kyu-Chan Shim ◽  
Sun Ha Kim ◽  
Yun-A Jeon ◽  
Hyun-Sook Lee ◽  
Cheryl Adeva ◽  
...  
Keyword(s):  
Chlorophyll Content ◽  
Leaf Senescence ◽  
Ubiquitin Ligase ◽  
Oryza Sativa L ◽  
Interspecific Cross ◽  
E3 Ubiquitin Ligase ◽  
Knockout Mutant ◽  
Ring Type ◽  
Delayed Senescence ◽  
F2 Population

Leaf senescence is the final stage of plant development. Many internal and external factors affect the senescence process in rice (Oryza sativa L.). In this study, we identified qCC2, a major quantitative trait locus (QTL) for chlorophyll content using a population derived from an interspecific cross between O. sativa (cv. Hwaseong) and Oryza grandiglumis. The O. grandiglumis allele at qCC2 increased chlorophyll content and delayed senescence. GW2 encoding E3 ubiquitin ligase in the qCC2 region was selected as a candidate for qCC2. To determine if GW2 is allelic to qCC2, a gw2-knockout mutant (gw2-ko) was examined using a dark-induced senescence assay. gw2-ko showed delayed leaf senescence in the dark with down-regulated expression of senescence-associated genes (SAGs) and chlorophyll degradation genes (CDGs). The association of the GW2 genotype with the delayed senescence phenotype was confirmed in an F2 population. RNA-seq analysis was conducted to investigate 30-day-old leaf transcriptome dynamics in Hwaseong and a backcross inbred line—CR2002—under dark treatment. This resulted in the identification of genes involved in phytohormone signaling and associated with senescence. These results suggested that transcriptional regulation was associated with delayed senescence in CR2002, and RING-type E3 ubiquitin ligase GW2 was a positive regulator of leaf senescence in rice.

Arabidopsis RING‐type E3 ubiquitin ligase XBAT35.2 promotes proteasome‐dependent degradation of ACD11 to attenuate abiotic stress tolerance

2020 ◽  
Vol 104 (6) ◽  
pp. 1712-1723
Author(s):  
Qiaomu Li ◽  
Renata J. Serio ◽  
Andrew Schofield ◽  
Hongxia Liu ◽  
Sheena R. Rasmussen ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Stress Tolerance ◽  
Ubiquitin Ligase ◽  
Abiotic Stress Tolerance ◽  
E3 Ubiquitin Ligase ◽  
Ring Type

scholarly journals Cbl-b, a RING-type E3 Ubiquitin Ligase, Targets Phosphatidylinositol 3-Kinase for Ubiquitination in T Cells

2000 ◽  
Vol 276 (7) ◽  
pp. 4872-4878 ◽  
Author(s):  
Deyu Fang ◽  
Hong-Ying Wang ◽  
Nan Fang ◽  
Yoav Altman ◽  
Chris Elly ◽  
...  
Keyword(s):  
T Cells ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Phosphatidylinositol 3 Kinase ◽  
Ring Type ◽  
Phosphatidylinositol 3

A QTL for rice grain width and weight encodes a previously unknown RING-type E3 ubiquitin ligase

2007 ◽  
Vol 39 (5) ◽  
pp. 623-630 ◽  
Author(s):  
Xian-Jun Song ◽  
Wei Huang ◽  
Min Shi ◽  
Mei-Zhen Zhu ◽  
Hong-Xuan Lin
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Rice Grain ◽  
Ring Type ◽  
Grain Width

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.

GmRFP1 encodes a previously unknown RING-type E3 ubiquitin ligase in Soybean (Glycine max)

2009 ◽  
Vol 37 (2) ◽  
pp. 685-693 ◽  
Author(s):  
Qiu-Li Du ◽  
Wen-Zhuo Cui ◽  
Chun-Hong Zhang ◽  
De-Yue Yu
Keyword(s):  
Glycine Max ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Type

scholarly journals The Molecular and Pathophysiological Functions of Members of the LNX/PDZRN E3 Ubiquitin Ligase Family

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 5938
Author(s):  
Jeongkwan Hong ◽  
Minho Won ◽  
Hyunju Ro
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ubiquitin Ligases ◽  
Ubiquitin Proteasome System ◽  
E3 Ubiquitin Ligases ◽  
Intercellular Signaling ◽  
Cellular Functions ◽  
Ring Type ◽  
Ubiquitin Ligase Activity ◽  
Ubiquitin Proteasome

The ligand of Numb protein-X (LNX) family, also known as the PDZRN family, is composed of four discrete RING-type E3 ubiquitin ligases (LNX1, LNX2, LNX3, and LNX4), and LNX5 which may not act as an E3 ubiquitin ligase owing to the lack of the RING domain. As the name implies, LNX1 and LNX2 were initially studied for exerting E3 ubiquitin ligase activity on their substrate Numb protein, whose stability was negatively regulated by LNX1 and LNX2 via the ubiquitin-proteasome pathway. LNX proteins may have versatile molecular, cellular, and developmental functions, considering the fact that besides these proteins, none of the E3 ubiquitin ligases have multiple PDZ (PSD95, DLGA, ZO-1) domains, which are regarded as important protein-interacting modules. Thus far, various proteins have been isolated as LNX-interacting proteins. Evidence from studies performed over the last two decades have suggested that members of the LNX family play various pathophysiological roles primarily by modulating the function of substrate proteins involved in several different intracellular or intercellular signaling cascades. As the binding partners of RING-type E3s, a large number of substrates of LNX proteins undergo degradation through ubiquitin-proteasome system (UPS) dependent or lysosomal pathways, potentially altering key signaling pathways. In this review, we highlight recent and relevant findings on the molecular and cellular functions of the members of the LNX family and discuss the role of the erroneous regulation of these proteins in disease progression.

scholarly journals A substrate-trapping strategy to find E3 ubiquitin ligase substrates identifies Parkin and TRIM28 targets

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Masashi Watanabe ◽  
Yasushi Saeki ◽  
Hidehisa Takahashi ◽  
Fumiaki Ohtake ◽  
Yukiko Yoshida ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
E3 Ligase ◽  
S Phase ◽  
E3 Ligases ◽  
Ring Type ◽  
Ubiquitin Binding ◽  
Cyclin A2

Abstract The identification of true substrates of an E3 ligase is biologically important but biochemically difficult. In recent years, several techniques for identifying substrates have been developed, but these approaches cannot exclude indirect ubiquitination or have other limitations. Here we develop an E3 ligase substrate-trapping strategy by fusing a tandem ubiquitin-binding entity (TUBE) with an anti-ubiquitin remnant antibody to effectively identify ubiquitinated substrates. We apply this method to one of the RBR-type ligases, Parkin, and to one of the RING-type ligases, TRIM28, and identify previously unknown substrates for TRIM28 including cyclin A2 and TFIIB. Furthermore, we find that TRIM28 promotes cyclin A2 ubiquitination and degradation at the G1/S phase and suppresses premature entry into S phase. Taken together, the results indicate that this method is a powerful tool for comprehensively identifying substrates of E3 ligases.

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