Arginyltransferase Is an ATP-Independent Self-Regulating Enzyme that Forms Distinct Functional Complexes In Vivo

Wang, Junling; Han, Xuemei; Saha, Swati; Xu, Tao; Rai, Reena; Zhang, Fangliang; Wolf, Yuri I.; Wolfson, Alexey D.; Yates, John R.; Kashina, Anna

doi:10.1016/j.chembiol.2010.10.016

Cited by 72 publications

(105 citation statements)

References 28 publications

(56 reference statements)

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“…Basal ATE function can be reconstituted in vitro, is independent of co-factors and requires only charged arginyl-tRNA and a substrate (12). Nevertheless, an increase of arginylation efficiency was observed upon addition of cell lysates in the same study, suggesting the presence of interaction partners or supporting co-factors.…”

mentioning

confidence: 79%

Identification of Targets and Interaction Partners of Arginyl-tRNA Protein Transferase in the Moss Physcomitrella patens

Hoernstein

Mueller

Fiedler

et al. 2016

Molecular & Cellular Proteomics

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Protein arginylation is a posttranslational modification of both N-terminal amino acids of proteins and sidechain carboxylates and can be crucial for viability and physiology in higher eukaryotes. The lack of arginylation causes severe developmental defects in moss, affects the low oxygen response in Arabidopsis thaliana and is embryo lethal in Drosophila and in mice. Although several studies investigated impact and function of the responsible enzyme, the arginyltRNA protein transferase (ATE) in plants, identification of arginylated proteins by mass spectrometry was not hitherto achieved. In the present study, we report the identification of targets and interaction partners of ATE in the model plant Physcomitrella patens by mass spectrometry, employing two different immuno-affinity strategies and a recently established transgenic ATE:GUS reporter line (Schuessele et al., 2016 New Phytol., DOI: 10.1111/nph.13656). Here we use a commercially available antibody against the fused reporter protein (␤-glucuronidase) to pull down ATE and its interacting proteins and validate its in vivo interaction with a class I small heatshock protein via Fö rster resonance energy transfer (FRET). Additionally, we apply and modify a method that already successfully identified arginylated proteins from mouse proteomes by using custom-made antibodies specific for N-terminal arginine. As a result, we identify four arginylated proteins from Physcomitrella patens with high confidence.

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mentioning

confidence: 79%

Identification of Targets and Interaction Partners of Arginyl-tRNA Protein Transferase in the Moss Physcomitrella patens

Hoernstein

Mueller

Fiedler

et al. 2016

Molecular & Cellular Proteomics

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“…However, our intuition guided us to work on the various aspects of the possible role of ATE1 in higher eukaryotes, despite the fact that essentiality was not established at that time. This intuition turned out to be correct, and arginylation is now well accepted to be just as important as the phosphorylation [26,27]. The very first work, which clearly established the essential nature of ATE1 in mammals, is the experiment where the ATE1 gene was knocked out in mice, causing lethality due to heart defects in cardiovascular development and angiogenic remodeling during embryogenesis [28].…”

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confidence: 99%

Global cellular regulation including cardiac function by post-translational protein arginylation

Kaji

2012

Journal of Molecular and Cellular Cardiology

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“…Degradation of the Glu 455 -Rec8 fragment was also assayed directly, using 35 S-pulse-chases and the URT, derived from the Ub fusion technique (Fig. 5C) (4, 21, 22, 91, 92).…”

Section: Arginylation-mediated Degradation Of the Separase-produced Rec8mentioning

confidence: 99%

“…URT-based 35 S-pulse-chases with C-terminally FLAGtagged Glu 455 -Rec8 f and its derivatives were performed in a transcription-translation-enabled rabbit reticulocyte extract, which contains the Arg/N-end rule pathway and has been extensively used to analyze this pathway (4,21,22). The indicated f DHFR-Ub R48 -X 455 -Rec8 f URT fusions (where X represents Glu, Val, or Arg-Glu) were labeled with […”

Section: Arginylation-mediated Degradation Of the Separase-produced Rec8mentioning

confidence: 99%

Degradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway

Liu

Chang

et al. 2016

Journal of Biological Chemistry

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The N-end rule pathway is a set of proteolytic systems whose unifying feature is the ability to recognize and polyubiquitylate proteins containing degradation signals called N-degrons, 6 thereby causing degradation of these proteins by the proteasome (Fig. 1, A and B) (1-8). The main determinant of an N-degron is either an unmodified or chemically modified destabilizing N-terminal residue of a protein. The identity of the next residue, at position 2, is often important as well. A second determinant of an N-degron is a protein's internal Lys residue. It functions as the site of a protein's polyubiquitylation and tends to be located in a conformationally disordered region (4, 9, 10). Recognition components of the N-end rule pathway are called N-recognins. In eukaryotes, N-recognins are E3 ubiquitin (Ub) ligases that can target N-degrons (Fig. 1, A and B). Bacteria also contain the N-end rule pathway, but Ub-independent versions of it (11-16).Regulated degradation of proteins and their natural fragments by the N-end rule pathway has been shown to mediate a strikingly broad range of biological functions, including the sensing of heme, nitric oxide (NO), oxygen, and short peptides; the control, through subunit-selective degradation, of the input stoichiometries of subunits in oligomeric protein complexes; the elimination of misfolded or otherwise abnormal proteins; the degradation of specific proteins after their retrotranslocation to the cytosol from mitochondria or other membrane-enclosed compartments; the regulation of apoptosis and repression of neurodegeneration; the regulation of DNA repair, transcription, replication, and chromosome cohesion/segregation; the regulation of G proteins, autophagy, peptide import, meiosis, immunity, fat metabolism, cell migration, actin filaments, cardiovascular development, spermatogenesis, and neurogenesis; the functioning of adult organs, including the brain, muscle, testis, and pancreas; and the regulation of leaf and shoot development, leaf senescence, and many other processes in plants (Fig. 1, A and B) (see Refs. 4 -7 and references therein).In eukaryotes, the N-end rule pathway consists of two branches. One branch, called the Ac/N-end rule pathway, targets proteins for degradation through their N ␣ -terminally acetylated (Nt-acetylated) residues (Fig. 1B) (2, 3, 17-19). Degradation signals and E3 Ub ligases of the Ac/N-end rule pathway are called Ac/N-degrons and Ac/N-recognins, respectively. Nt-acetylation of cellular proteins is apparently irreversible, * This work was supported by National Natural Science Foundation of China Grants 31171374 and 31471277 and Major Basic Research Program Grant 2012CB944404 (to W. L.) and by National Institutes of Health Grants R01-DK039520 and R01-GM031530 (to A. V.). The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. 1 These authors contribut...

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Arginyltransferase Is an ATP-Independent Self-Regulating Enzyme that Forms Distinct Functional Complexes In Vivo

Cited by 72 publications

References 28 publications

Identification of Targets and Interaction Partners of Arginyl-tRNA Protein Transferase in the Moss Physcomitrella patens

Identification of Targets and Interaction Partners of Arginyl-tRNA Protein Transferase in the Moss Physcomitrella patens

Global cellular regulation including cardiac function by post-translational protein arginylation

Degradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway

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