AtCHIP, a U-Box-Containing E3 Ubiquitin Ligase, Plays a Critical Role in Temperature Stress Tolerance in Arabidopsis

Yan, Jun; Wang, Jing; Li, Qingtian; Hwang, Jae Ryoung; Patterson, Cam; Zhang, Hong

doi:10.1104/pp.103.020800

Cited by 160 publications

(158 citation statements)

References 33 publications

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“…7 and 8). The more sensitive phenotype of 35STCaPUB1 lines to drought and salinity is reminiscent of the Arabidopsis U-box AtCHIP-overexpressing plants, which are hypersensitive to extreme temperatures, indicating that increased AtCHIP or CaPUB1 alone might not be enough for enhancing stress tolerance (Yan et al, 2003). Closer inspection revealed that the individual transgenic roots had increased numbers of small-sized cells around the cortex, endodermis, and stele, resulting in disordered, highly populated cell layers relative to control roots (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…A previous study showed that the Arabidopsis U-box AtCHIP transcript was induced significantly by extreme temperatures (Yan et al, 2003). Overexpression of AtCHIP rendered Arabidopsis plants more sensitive to both low and high temperatures Yan et al, 2003). AtCHIP was subsequently reported to interact with an A-subunit of protein phosphatase 2A and suggested to be involved in the ABA-related stress-signaling pathway (Luo et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Heterologous Expression and Molecular and Cellular Characterization of CaPUB1 Encoding a Hot Pepper U-Box E3 Ubiquitin Ligase Homolog

et al. 2006

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The U-box motif is a conserved domain found in the diverse isoforms of E3 ubiquitin ligase in eukaryotes. From water-stressed hot pepper (Capsicum annuum L. cv Pukang) plants, we isolated C. annuum putative U-box protein 1 (CaPUB1), which encodes a protein containing a single U-box motif in its N-terminal region. In vitro ubiquitination and site-directed mutagenesis assays revealed that CaPUB1 possessed E3 ubiquitin ligase activity and that the U-box motif was indeed essential for its enzyme activity. RNA gel-blot analysis showed that CaPUB1 mRNA was induced rapidly by a broad spectrum of abiotic stresses, including drought, high salinity, cold temperature, and mechanical wounding, but not in response to ethylene, abscisic acid, or a bacterial pathogen, suggesting its role in the early events in the abiotic-related defense response. Because transgenic work was extremely difficult in hot pepper, in this study we overexpressed CaPUB1 in Arabidopsis (Arabidopsis thaliana) to provide cellular information on the function of this gene in the development and plant responses to abiotic stresses. Transgenic Arabidopsis plants that constitutively expressed the CaPUB1 gene under the control of the cauliflower mosaic virus 35S promoter had markedly longer hypocotyls and roots and grew more rapidly than the wild type, leading to an early bolting phenotype. Microscopic analysis showed that 35STCaPUB1 roots had increased numbers of small-sized cells, resulting in disordered, highly populated cell layers in the cortex, endodermis, and stele. In addition, CaPUB1-overexpressing plants displayed increased sensitivity to water stress and mild salinity. These results indicate that CaPUB1 is functional in Arabidopsis cells, thereby effectively altering cell and tissue growth and also the response to abiotic stresses. Comparative proteomic analysis showed that the level of RPN6 protein, a non-ATPase subunit of the 26S proteasome complex, was significantly reduced in 35STCaPUB1 seedlings as compared to the wild type. Pull-down and ubiquitination assays demonstrated that RPN6 interacted physically with CaPUB1 and was ubiquitinated in a CaPUB1-dependent manner in vitro. Although the physiological function of CaPUB1 is not yet clear, there are several possibilities for its involvement in a subset of physiological responses to counteract dehydration and high-salinity stresses in transgenic Arabidopsis seedlings.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Heterologous Expression and Molecular and Cellular Characterization of CaPUB1 Encoding a Hot Pepper U-Box E3 Ubiquitin Ligase Homolog

et al. 2006

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“…CHIP was also found to be able to promote formation of Lys63-linked polyubiquitin chains in collaboration with Uev1a-Ubc13 in vitro [75]. In plants, the Arabidopsis CHIP gene AtCHIP is upregulated upon temperature stress [76]. However, overexpression of AtCHIP in Arabidopsis rendered plants more sensitive to both low-and high-temperature treatments, suggesting that CHIP's function in plants is complex and it warrants further detailed characterization.…”

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

confidence: 98%

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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“…In contrast, the homology of this protein to the TPR motifs of hCHIP is very weak, and it does not contain a mixed charge region. It nevertheless seems to function as a bona fide CHIP protein (9). No CHIP homologues exist in Saccharomyces cerevisiae and Schizosaccharomyces pombe.…”

mentioning

confidence: 99%

Dimerization of the Human E3 Ligase CHIP via a Coiled-coil Domain Is Essential for Its Activity

Nikolay¹,

Wiederkehr²,

Rist

et al. 2004

Journal of Biological Chemistry

107

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The Hsp70-interacting E3-ubiquitin ligase CHIP has been implicated in the decision as to whether a target protein enters the refolding or the degradation pathway. To further characterize the activity of CHIP we purified untagged Homo sapiens and Drosophila melanogaster CHIP (hCHIP, dCHIP). In contrast to other E3-ubiquitin ligases, both hCHIP and dCHIP proteins formed homodimers at physiological concentrations. We identified a predicted coiled-coil region in a mixed charge segment of the hCHIP and dCHIP sequence and found it to be necessary and sufficient for dimer formation. A mutant of hCHIP lacking this segment (hCHIP⌬-(128 -229)) was incapable of dimer formation, but the segment by itself (hCHIP-(128 -229)) readily dimerized. Furthermore, we demonstrated that dimerization is a prerequisite for activity of hCHIP in the reconstituted ubiquitination assay. Control of dimerization may thus provide a mechanism for regulation of CHIP activity.

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AtCHIP, a U-Box-Containing E3 Ubiquitin Ligase, Plays a Critical Role in Temperature Stress Tolerance in Arabidopsis

Cited by 160 publications

References 33 publications

Heterologous Expression and Molecular and Cellular Characterization of CaPUB1 Encoding a Hot Pepper U-Box E3 Ubiquitin Ligase Homolog

Heterologous Expression and Molecular and Cellular Characterization of CaPUB1 Encoding a Hot Pepper U-Box E3 Ubiquitin Ligase Homolog

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

Dimerization of the Human E3 Ligase CHIP via a Coiled-coil Domain Is Essential for Its Activity

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