A recessive mutation in the RUB1‐conjugating enzyme, RCE1, reveals a requirement for RUB modification for control of ethylene biosynthesis and proper induction of basic chitinase and PDF1.2 in Arabidopsis

Larsen, Paul B.; Cancel, Jesse D.

doi:10.1111/j.1365-313x.2004.02068.x

Cited by 51 publications

(47 citation statements)

References 43 publications

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“…These results are consistent with the possibility that ecr1-1 defects in root elongation in the light and hypocotyl elongation in the dark result from ethylene overproduction. Interestingly, rub1 rub2 RNAi lines and rce1 mutant seedlings overproduce ethylene, whereas axr1 seedlings have slightly reduced ethylene levels (Bostick et al, 2004;Larsen and Cancel, 2004); our data suggest that ecr1-1 more closely resembles rub and rce1 than axr1 in ethylene physiology.…”

Section: Cullin Modification Is Defective In Ecr1-1mentioning

confidence: 69%

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Mutation ofE1-CONJUGATING ENZYME-RELATED1Decreases RELATED TO UBIQUITIN Conjugation and Alters Auxin Response and Development

et al. 2007

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The ubiquitin-like protein RELATED TO UBIQUITIN (RUB) is conjugated to CULLIN (CUL) proteins to modulate the activity of Skp1-Cullin-F-box (SCF) ubiquitylation complexes. RUB conjugation to specific target proteins is necessary for the development of many organisms, including Arabidopsis (Arabidopsis thaliana). Here, we report the isolation and characterization of e1-conjugating enzyme-related1-1 (ecr1-1), an Arabidopsis mutant compromised in RUB conjugation. The ecr1-1 mutation causes a missense change located two amino acid residues from the catalytic site cysteine, which normally functions to form a thioester bond with activated RUB. A higher ratio of unmodified CUL1 relative to CUL1-RUB is present in ecr1-1 compared to wild type, suggesting that the mutation reduces ECR1 function. The ecr1-1 mutant is resistant to the auxin-like compound indole-3-propionic acid, produces fewer lateral roots than wild type, displays reduced adult height, and stabilizes a reporter fusion protein that is degraded in response to auxin, suggesting reduced auxin signaling in the mutant. In addition, ecr1-1 hypocotyls fail to elongate normally when seedlings are grown in darkness, a phenotype shared with certain other RUB conjugation mutants that is not general to auxin-response mutants. The suite of ecr1-1 molecular and morphological phenotypes reflects roles for RUB conjugation in many aspects of plant growth and development. Certain ecr1-1 elongation defects are restored by treatment with the ethylene-response inhibitor silver nitrate, suggesting that the short ecr1-1 root and hypocotyl result from aberrant ethylene accumulation. Further, silver nitrate supplementation in combination with various auxins and auxin-like compounds reveals that members of this growth regulator family may differentially rely on ethylene signaling to inhibit root growth.

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Section: Cullin Modification Is Defective In Ecr1-1mentioning

confidence: 69%

“…Like ecr1-1 (Figs. 1A and 2), loss-of-function mutants defective in other components of the RUB modification system, including axr1, rce1, and rub1 rub2 RNAi lines, are also resistant to certain auxins (Estelle and Somerville, 1987;Dharmasiri et al, 2003b;Bostick et al, 2004;Larsen and Cancel, 2004).…”

Section: Discussionmentioning

confidence: 99%

Mutation ofE1-CONJUGATING ENZYME-RELATED1Decreases RELATED TO UBIQUITIN Conjugation and Alters Auxin Response and Development

et al. 2007

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“…Rub1/Nedd8 and consequently its conjugation pathway are required for the SCF E3 activity [85,86]. Mutation of RCE1 (RUB-conjugating enzyme1) resulted in defects in the expression of defense-related genes' basic chitinase and PDF1.2, inferring that the SCF E3 complex it modified is required for plant defense [87]. RCE1 was shown in Arabidopsis to be part of a stable SCF TIR ubiquitin E3 ligase complex [88], which is a critical component in plant auxin signaling [89][90][91].…”

Section: U-box-type E3 Ligases Are Newly Identified Members Of the Ubmentioning

confidence: 99%

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

et al. 2006

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Post-translational modification is central to protein stability and to the modulation of protein activity. Various types of protein modification, such as phosphorylation, methylation, acetylation, myristoylation, glycosylation, and ubiquitination, have been reported. Among them, ubiquitination distinguishes itself from others in that most of the ubiquitinated proteins are targeted to the 26S proteasome for degradation. The ubiquitin/26S proteasome system constitutes the major protein degradation pathway in the cell. In recent years, the importance of the ubiquitination machinery in the control of numerous eukaryotic cellular functions has been increasingly appreciated. Increasing number of E3 ubiquitin ligases and their substrates, including a variety of essential cellular regulators have been identified. Studies in the past several years have revealed that the ubiquitination system is important for a broad range of plant developmental processes and responses to abiotic and biotic stresses. This review discusses recent advances in the functional analysis of ubiquitination-associated proteins from plants and pathogens that play important roles in plant-microbe interactions.

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“…Like the ubiquitin pathway, the RUB conjugation pathway is catalyzed by enzymatic cascade and is essential in Schizosaccharomyces pombe, Caenorhabditis elegans, Drosophila, and mouse (Jones and Candido, 2000;Osaka et al, 2000;Tateishi et al, 2001;Ou et al, 2002;Lykke-Andersen et al, 2003). Rubylation also plays an important role in many plant processes including embryo development and auxin and ethylene responses (del Pozo et al, 2002;Dharmasiri et al, 2003;Larsen and Cancel, 2004).…”

Section: Introductionmentioning

confidence: 99%

The Arabidopsis CSN5A and CSN5B Subunits Are Present in Distinct COP9 Signalosome Complexes, and Mutations in Their JAMM Domains Exhibit Differential Dominant Negative Effects on Development

2004

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The COP9 signalosome (CSN) is an evolutionarily conserved multisubunit protein complex involved in a variety of signaling and developmental processes through the regulation of protein ubiquitination and degradation. A known biochemical role attributed to CSN is a metalloprotease activity responsible for the derubylation of cullins, core components for several types of ubiquitin E3 ligases. The CSN's derubylation catalytic center resides in its subunit 5, which in Arabidopsis thaliana is encoded by two homologous genes, CSN5A and CSN5B. Here, we show that CSN5A and CSN5B subunits are assembled into distinct CSN complexes in vivo, which are present in drastically different abundances, with CSN CSN5A appearing to be the dominant one. Transgenic CSN5A and CSN5B proteins carrying a collection of single mutations in or surrounding the metalloprotease catalytic center are properly assembled into CSN complexes, but only mutations in CSN5A result in a pleiotropic dominant negative phenotype. The extent of phenotypic effects caused by mutations in CSN5A is reflected at the molecular level by impairment in Cullin1 derubylation. These results reveal that three key metal binding residues as well as two other amino acids outside the catalytic center play important roles in CSN derubylation activity. Taken together, our data provide physiological evidence on a positive role of CSN in the regulation of Arabidopsis SCF (for Skp1-Cullin-F-box) E3 ligases through RUB (for Related to Ubiquitin) deconjugation and highlight the unequal role that CSN CSN5A and CSN CSN5B play in controlling the cellular derubylation of cullins. The initial characterization of CSN5A and CSN5B insertion mutants further supports these findings and provides genetic evidence on their unequal role in plant development.

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A recessive mutation in the RUB1‐conjugating enzyme, RCE1, reveals a requirement for RUB modification for control of ethylene biosynthesis and proper induction of basic chitinase and PDF1.2 in Arabidopsis

Cited by 51 publications

References 43 publications

Mutation ofE1-CONJUGATING ENZYME-RELATED1Decreases RELATED TO UBIQUITIN Conjugation and Alters Auxin Response and Development

Mutation ofE1-CONJUGATING ENZYME-RELATED1Decreases RELATED TO UBIQUITIN Conjugation and Alters Auxin Response and Development

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

The Arabidopsis CSN5A and CSN5B Subunits Are Present in Distinct COP9 Signalosome Complexes, and Mutations in Their JAMM Domains Exhibit Differential Dominant Negative Effects on Development

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