Glyoxylate Reductase Isoform 1 is Localized in the Cytosol and Not Peroxisomes in Plant Cells

Ching, Steven L. K.; Gidda, Satinder K.; Rochon, Amanda; Cauwenberghe, Owen R. Van; Shelp, Barry J.; Mullen, Robert T.

doi:10.1111/j.1744-7909.2012.01103.x

Cited by 35 publications

(35 citation statements)

References 92 publications

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“…Asterisks indicate the relevant bands. Ching et al, 2012) in N. tabacum suspension-cultured cells (Supplemental Fig. S3B), reconfirming that the XBAT35.2-containing structures were Golgi and not peroxisomes, which generally can resemble one another based on their appearance via confocal microscopy.…”

Section: Xbat352 Localizes Predominantly To the Golgi In Arabidopsismentioning

confidence: 74%

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The RING-Type E3 Ligase XBAT35.2 Is Involved in Cell Death Induction and Pathogen Response

et al. 2017

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XBAT35 belongs to a subfamily of Arabidopsis (Arabidopsis thaliana) RING-type E3s that are similar in domain architecture to the rice (Oryza sativa) XA21 Binding Protein3, a defense protein. The XBAT35 transcript undergoes alternative splicing to produce two protein isoforms, XBAT35.1 and XBAT35.2. Here, we demonstrate that XBAT35.2 localizes predominantly to the Golgi and is involved in cell death induction and pathogen response. XBAT35.2, but not XBAT35.1, was found to trigger cell death when overexpressed in tobacco (Nicotiana benthamiana) leaves and does so in a manner that requires its RING domain. Loss of XBAT35 gene function disrupts the plant's ability to defend against pathogen attack, whereas overexpression of XBAT35.2 enhances resistance to pathogens. XBAT35.2 was found to be unstable and promotes its own degradation, suggesting self-regulation. Inoculation with virulent and avirulent strains of the bacterial pathogen Pseudomonas syringae pv tomato DC3000 results in a drastic reduction in the levels of ubiquitinated XBAT35.2 and an increase in the abundance of the E3. This implies that pathogen infection prohibits XBAT35.2 self-regulation and stabilizes the E3. In agreement with a role in defending against pathogens, XBAT35.2 interacts with defense-related Accelerated Cell Death11 (ACD11) in planta and promotes the proteasome-dependent turnover of ACD11 in cell-free degradation assays. In accordance with regulation by a stabilized XBAT35.2, the levels of ubiquitinated ACD11 increased considerably, and the abundance of ACD11 was reduced following pathogen infection. In addition, treatment of transgenic seedlings with a proteasome inhibitor results in the accumulation of ACD11, confirming proteasome-dependent degradation. Collectively, these results highlight a novel role for XBAT35.2 in cell death induction and defense against pathogens.Posttranslational modification (PTM) via ubiquitination plays essential regulatory roles in all eukaryotic cells. The selective attachment of ubiquitin serves as a versatile modification that regulates protein activity, abundance, sorting, and localization (Deshaies and Joazeiro, 2009;Komander and Rape, 2012). This versatility places ubiquitination at the center of numerous cellular processes and allows for the regulation of growth, development, and responses to various environmental stimuli. Ubiquitination is accomplished through the sequential action of three enzymes: E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin ligase). Ubiquitin conjugation begins with the activation of ubiquitin molecules by E1, which is then transferred to E2, forming a thioester-linked E2-ubiquitin intermediate. Finally, E3 mediates the transfer of ubiquitin from the E2-ubiquitin intermediate to the substrate. The covalent attachment of ubiquitin to the substrate is usually accomplished via the formation of an isopeptide bond between the C-terminal Gly of ubiquitin and an internal lysine (Lys) of the substrate. Substrate modifications include the

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Section: Xbat352 Localizes Predominantly To the Golgi In Arabidopsismentioning

confidence: 74%

“…pMDC32/Cherry-PTS1, consisting of the Cherry red fluorescent protein linked to a C-terminal type 1 peroxisomal targeting signal, has been described elsewhere (Ching et al, 2012). Constructs were introduced into tobacco leaves or suspension cell cultures as described above.…”

Section: Subcellular Localizationmentioning

confidence: 99%

The RING-Type E3 Ligase XBAT35.2 Is Involved in Cell Death Induction and Pathogen Response

et al. 2017

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“…Preferentially, GLYR1 catalyzes the NADPH-based reduction of glyoxylate into glycolate, and it has been proposed that glyoxylate detoxification by GLYR1 could provide an alternative sink for excess electrons during the recycling of reducing equivalents (121). Yet recently it was shown that the GLYR1 protein is exclusively present in the cytosol and is not found in the peroxisome (122). As GABA is converted to succinate semialdehyde in the mitochondria, GLYR1 could thus be involved in the detoxification of glyoxylate that accidently reaches the cytosol.…”

Section: Constitutive De Novo Synthesis Of Enzymes Involved In Energymentioning

confidence: 99%

Dynamic Proteomics Emphasizes the Importance of Selective mRNA Translation and Protein Turnover during Arabidopsis Seed Germination

Galland¹,

Huguet²,

Arc³

et al. 2014

Molecular & Cellular Proteomics

146

155

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During seed germination, the transition from a quiescent metabolic state in a dry mature seed to a proliferative metabolic state in a vigorous seedling is crucial for plant propagation as well as for optimizing crop yield. This work provides a detailed description of the dynamics of protein synthesis during the time course of germination, demonstrating that mRNA translation is both sequential and selective during this process. The complete inhibition of the germination process in the presence of the translation inhibitor cycloheximide established that mRNA translation is critical for Arabidopsis seed germination. However, the dynamics of protein turnover and the selectivity of protein synthesis (mRNA translation) during Arabidopsis seed germination have not been addressed yet. Based on our detailed knowledge of the Arabidopsis seed proteome, we have deepened our understanding of seed mRNA translation during germination by combining twodimensional gel-based proteomics with dynamic radiolabeled proteomics using a radiolabeled amino acid precursor, namely [35 S]-methionine, in order to highlight de novo protein synthesis, stability, and turnover. Our data confirm that during early imbibition, the Arabidopsis translatome keeps reflecting an embryonic maturation program until a certain developmental checkpoint. Furthermore, by dividing the seed germination time lapse into discrete time windows, we highlight precise and specific patterns of protein synthesis. These data refine and deepen our knowledge of the three classical phases of seed germination based on seed water uptake during imbibition and reveal that selective mRNA translation is a key feature of seed germination. Beyond the quantitative control of translational activity, both the selectivity of mRNA translation and protein turnover appear as specific regulatory systems, critical for timing the molecular events leading to successful germination and seedling establishment. Molecular & Cellular Proteomics 13: 10.1074/mcp.M113.032227, 252-268, 2014.Seed germination is a vital stage in the plant life cycle during which embryo cells experience a programmed transition from a quiescent to a highly active metabolic state. Accordingly, seed quality in terms of germination vigor is of paramount importance for both ecological aspects and practical applications, as it influences the level, timing, and uniformity of seedling emergence in a wide range of environmental conditions (1, 2). In efforts to decipher the complex molecular mechanisms that control seed germination, genetic, genomic, and postgenomic analyses have been developed on the model plant Arabidopsis thaliana (3-6). Germination is classically described as a sequential time course divided into three major phases of seed water uptake (7). Phase I is characterized by rapid seed imbibition, which is crucial for the transition from the quiescent metabolic state of the dry seed to the high metabolic activity of the hydrated seed. Phase II corresponds to a period during which the seed imbibition level remains const...

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“…Other previously described plant expression vectors include the following plasmids: pRTL2/RFP, encoding the red fluorescent protein (RFP) (36); pUC18/GFP-Syp21 and pUC18/GFPSyp52, which encode GFP fused to the N termini of the Arabidopsis membrane-bound Qa-SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) Syp21 (Syntaxin of plants 21) and Syp52 (37) proteins (kindly provided by M. Sato [Kyoto University]); pSAT2/Cherry-PTS1, encoding the monomeric cherry fluorescent protein fused to the C-terminal 10 amino acid residues of pumpkin hydroxypyruvate reductase, including its type 1 peroxisomal targeting signal (38); pRTL2/TIC40-RFP, encoding the Arabidopsis 40-kDa component of the translocon at the inner membrane of chloroplasts fused to the N terminus of RFP (39); and pSAT4A/AtPAP26-mCherry, encoding the Arabidopsis purple acid phosphatase isoform 26 fused to the N terminus of the monomeric cherry fluorescent protein (40). Yeast two-hybrid expression vectors, pGADT7 and pGBKT7 (Clontech) encoding Arabidopsis Vps23, Vps25, Vps37, and Vps28 were also previously described (35).…”

Section: Methodsmentioning

confidence: 99%

A Unique N-Terminal Sequence in the Carnation Italian ringspot virus p36 Replicase-Associated Protein Interacts with the Host Cell ESCRT-I Component Vps23

Richardson

Clendening

Sheen

et al. 2014

J Virol

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Like most positive-strand RNA viruses, infection by plant tombusviruses results in extensive rearrangement of specific host cell organelle membranes that serve as the sites of viral replication. The tombusvirus Tomato bushy stunt virus (TBSV) replicates within spherules derived from the peroxisomal boundary membrane, a process that involves the coordinated action of various viral and cellular factors, including constituents of the endosomal sorting complex required for transport (ESCRT). ESCRT is comprised of a series of protein subcomplexes (i.e., ESCRT-0 -I, -II, and -III) that normally participate in late endosome biogenesis and some of which are also hijacked by certain enveloped retroviruses (e.g., HIV) for viral budding from the plasma membrane. Here we show that the replication of Carnation Italian ringspot virus (CIRV), a tombusvirus that replicates at mitochondrial membranes also relies on ESCRT. In plant cells, CIRV recruits the ESCRT-I protein, Vps23, to mitochondria through an interaction that involves a unique region in the N terminus of the p36 replicase-associated protein that is not conserved in TBSV or other peroxisome-targeted tombusviruses. The interaction between p36 and Vps23 also involves the Vps23 C-terminal steadiness box domain and not its N-terminal ubiquitin E2 variant domain, which in the case of TBSV (and enveloped retroviruses) mediates the interaction with ESCRT. Overall, these results provide evidence that CIRV uses a unique N-terminal sequence for the recruitment of Vps23 that is distinct from those used by TBSV and certain mammalian viruses for ESCRT recruitment. Characterization of this novel interaction with Vps23 contributes to our understanding of how CIRV may have evolved to exploit key differences in the plant ESCRT machinery. IMPORTANCEPositive-strand RNA viruses replicate their genomes in association with specific host cell membranes. To accomplish this, cellular components responsible for membrane biogenesis and modeling are appropriated by viral proteins and redirected to assemble membrane-bound viral replicase complexes. The diverse pathways leading to the formation of these replication structures are poorly understood. We have determined that the cellular ESCRT system that is normally responsible for mediating late endosome biogenesis is also involved in the replication of the tombusvirus Carnation Italian ringspot virus (CIRV) at mitochondria. Notably, CIRV recruits ESCRT to the mitochondrial outer membrane via an interaction between a unique motif in the viral protein p36 and the ESCRT component Vps23. Our findings provide new insights into tombusvirus replication and the virusinduced remodeling of plant intracellular membranes, as well as normal ESCRT assembly in plants.T ombusviruses are positive-strand RNA [(ϩ)RNA] viruses that infect a wide range of plant species and replicate at host cell membranes derived specifically from either peroxisomes (e.g., Tomato bushy stunt virus [TBSV]) or mitochondria (e.g., Carnation Italian ringspot virus [CIRV]) (1). Up...

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Glyoxylate Reductase Isoform 1 is Localized in the Cytosol and Not Peroxisomes in Plant Cells

Cited by 35 publications

References 92 publications

The RING-Type E3 Ligase XBAT35.2 Is Involved in Cell Death Induction and Pathogen Response

The RING-Type E3 Ligase XBAT35.2 Is Involved in Cell Death Induction and Pathogen Response

Dynamic Proteomics Emphasizes the Importance of Selective mRNA Translation and Protein Turnover during Arabidopsis Seed Germination

A Unique N-Terminal Sequence in the Carnation Italian ringspot virus p36 Replicase-Associated Protein Interacts with the Host Cell ESCRT-I Component Vps23

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