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Journal articles on the topic 'Wobble uridine modifications'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Johansson, Marcus J. O., Anders Esberg, Bo Huang, Glenn R. Björk, and Anders S. Byström. "Eukaryotic Wobble Uridine Modifications Promote a Functionally Redundant Decoding System." Molecular and Cellular Biology 28, no. 10 (2008): 3301–12. http://dx.doi.org/10.1128/mcb.01542-07.

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ABSTRACT The translational decoding properties of tRNAs are modulated by naturally occurring modifications of their nucleosides. Uridines located at the wobble position (nucleoside 34 [U34]) in eukaryotic cytoplasmic tRNAs often harbor a 5-methoxycarbonylmethyl (mcm5) or a 5-carbamoylmethyl (ncm5) side chain and sometimes an additional 2-thio (s2) or 2′-O-methyl group. Although a variety of models explaining the role of these modifications have been put forth, their in vivo functions have not been defined. In this study, we utilized recently characterized modification-deficient Saccharomyces c

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2

Songe-Møller, Lene, Erwin van den Born, Vibeke Leihne, et al. "Mammalian ALKBH8 Possesses tRNA Methyltransferase Activity Required for the Biogenesis of Multiple Wobble Uridine Modifications Implicated in Translational Decoding." Molecular and Cellular Biology 30, no. 7 (2010): 1814–27. http://dx.doi.org/10.1128/mcb.01602-09.

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ABSTRACT Uridines in the wobble position of tRNA are almost invariably modified. Modifications can increase the efficiency of codon reading, but they also prevent mistranslation by limiting wobbling. In mammals, several tRNAs have 5-methoxycarbonylmethyluridine (mcm5U) or derivatives thereof in the wobble position. Through analysis of tRNA from Alkbh8 −/− mice, we show here that ALKBH8 is a tRNA methyltransferase required for the final step in the biogenesis of mcm5U. We also demonstrate that the interaction of ALKBH8 with a small accessory protein, TRM112, is required to form a functional tRN

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3

Karlsborn, Tony, Hasan Tükenmez, A. K. M. Firoj Mahmud, Fu Xu, Hao Xu, and Anders S. Byström. "Elongator, a conserved complex required for wobble uridine modifications in Eukaryotes." RNA Biology 11, no. 12 (2014): 1519–28. http://dx.doi.org/10.4161/15476286.2014.992276.

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4

Schaffrath, Raffael, and Sebastian A. Leidel. "Wobble uridine modifications–a reason to live, a reason to die?!" RNA Biology 14, no. 9 (2017): 1209–22. http://dx.doi.org/10.1080/15476286.2017.1295204.

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5

Tükenmez, Hasan, Hao Xu, Anders Esberg, and Anders S. Byström. "The role of wobble uridine modifications in +1 translational frameshifting in eukaryotes." Nucleic Acids Research 43, no. 19 (2015): 9489–99. http://dx.doi.org/10.1093/nar/gkv832.

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6

Hawer, Harmen, Alexander Hammermeister, Keerthiraju Ravichandran, Sebastian Glatt, Raffael Schaffrath, and Roland Klassen. "Roles of Elongator Dependent tRNA Modification Pathways in Neurodegeneration and Cancer." Genes 10, no. 1 (2018): 19. http://dx.doi.org/10.3390/genes10010019.

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Transfer RNA (tRNA) is subject to a multitude of posttranscriptional modifications which can profoundly impact its functionality as the essential adaptor molecule in messenger RNA (mRNA) translation. Therefore, dynamic regulation of tRNA modification in response to environmental changes can tune the efficiency of gene expression in concert with the emerging epitranscriptomic mRNA regulators. Several of the tRNA modifications are required to prevent human diseases and are particularly important for proper development and generation of neurons. In addition to the positive role of different tRNA

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7

Wang, Hailang, Chao Xu, Youbing Zhang, et al. "PtKTI12 genes influence wobble uridine modifications and drought stress tolerance in hybrid poplar." Tree Physiology 40, no. 12 (2020): 1778–91. http://dx.doi.org/10.1093/treephys/tpaa088.

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ABSTRACT The multisubunit Elongator complex plays key roles in transcription by interacting with RNA polymerase II and chromatin modeling. Kti proteins have been identified as the auxiliary protein for the Elongator complex. However, our knowledge of Kti proteins in woody plants remains limited. In this study, in total 16 KTI gene homologs were identified in Populus trichocarpa. Among them, the two KTI12 candidates were named PtKTI12A and PtKTI12B. Although PtKTI12A and PtKTI12B were largely different in gene expression level and tissue specificity, both genes were induced by heat and drought

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8

Suzuki, Takeo, Kenjyo Miyauchi, Tsutomu Suzuki, et al. "Taurine-containing Uridine Modifications in tRNA Anticodons Are Required to Decipher Non-universal Genetic Codes in Ascidian Mitochondria." Journal of Biological Chemistry 286, no. 41 (2011): 35494–98. http://dx.doi.org/10.1074/jbc.m111.279810.

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Variations in the genetic code are found frequently in mitochondrial decoding systems. Four non-universal genetic codes are employed in ascidian mitochondria: AUA for Met, UGA for Trp, and AGA/AGG(AGR) for Gly. To clarify the decoding mechanism for the non-universal genetic codes, we isolated and analyzed mitochondrial tRNAs for Trp, Met, and Gly from an ascidian, Halocynthia roretzi. Mass spectrometric analysis identified 5-taurinomethyluridine (τm5U) at the anticodon wobble positions of tRNAMet(AUR), tRNATrp(UGR), and tRNAGly(AGR), suggesting that τm5U plays a critical role in the accurate d

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9

Gupta, Ritu, and Sunil Laxman. "tRNA wobble-uridine modifications as amino acid sensors and regulators of cellular metabolic state." Current Genetics 66, no. 3 (2019): 475–80. http://dx.doi.org/10.1007/s00294-019-01045-y.

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10

Fu, Dragony, Jennifer A. N. Brophy, Clement T. Y. Chan, et al. "Human AlkB Homolog ABH8 Is a tRNA Methyltransferase Required for Wobble Uridine Modification and DNA Damage Survival." Molecular and Cellular Biology 30, no. 10 (2010): 2449–59. http://dx.doi.org/10.1128/mcb.01604-09.

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ABSTRACT tRNA nucleosides are extensively modified to ensure their proper function in translation. However, many of the enzymes responsible for tRNA modifications in mammals await identification. Here, we show that human AlkB homolog 8 (ABH8) catalyzes tRNA methylation to generate 5-methylcarboxymethyl uridine (mcm5U) at the wobble position of certain tRNAs, a critical anticodon loop modification linked to DNA damage survival. We find that ABH8 interacts specifically with tRNAs containing mcm5U and that purified ABH8 complexes methylate RNA in vitro. Significantly, ABH8 depletion in human cell

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11

Klassen, Roland, Pia Grunewald, Kathrin L. Thüring, Christian Eichler, Mark Helm, and Raffael Schaffrath. "Loss of Anticodon Wobble Uridine Modifications Affects tRNALys Function and Protein Levels in Saccharomyces cerevisiae." PLOS ONE 10, no. 3 (2015): e0119261. http://dx.doi.org/10.1371/journal.pone.0119261.

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12

Delaunay, Sylvain, Francesca Rapino, Lars Tharun, et al. "Elp3 links tRNA modification to IRES-dependent translation of LEF1 to sustain metastasis in breast cancer." Journal of Experimental Medicine 213, no. 11 (2016): 2503–23. http://dx.doi.org/10.1084/jem.20160397.

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Quantitative and qualitative changes in mRNA translation occur in tumor cells and support cancer progression and metastasis. Posttranscriptional modifications of transfer RNAs (tRNAs) at the wobble uridine 34 (U34) base are highly conserved and contribute to translation fidelity. Here, we show that ELP3 and CTU1/2, partner enzymes in U34 mcm5s2-tRNA modification, are up-regulated in human breast cancers and sustain metastasis. Elp3 genetic ablation strongly impaired invasion and metastasis formation in the PyMT model of invasive breast cancer. Mechanistically, ELP3 and CTU1/2 support cellular

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13

Khonsari, Bahar, Roland Klassen, and Raffael Schaffrath. "Role of SSD1 in Phenotypic Variation of Saccharomyces cerevisiae Strains Lacking DEG1-Dependent Pseudouridylation." International Journal of Molecular Sciences 22, no. 16 (2021): 8753. http://dx.doi.org/10.3390/ijms22168753.

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Yeast phenotypes associated with the lack of wobble uridine (U34) modifications in tRNA were shown to be modulated by an allelic variation of SSD1, a gene encoding an mRNA-binding protein. We demonstrate that phenotypes caused by the loss of Deg1-dependent tRNA pseudouridylation are similarly affected by SSD1 allelic status. Temperature sensitivity and protein aggregation are elevated in deg1 mutants and further increased in the presence of the ssd1-d allele, which encodes a truncated form of Ssd1. In addition, chronological lifespan is reduced in a deg1 ssd1-d mutant, and the negative genetic

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14

Yoshida, Mayumi, Naoyuki Kataoka, Kenjyo Miyauchi, et al. "Rectifier of aberrant mRNA splicing recovers tRNA modification in familial dysautonomia." Proceedings of the National Academy of Sciences 112, no. 9 (2015): 2764–69. http://dx.doi.org/10.1073/pnas.1415525112.

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Familial dysautonomia (FD), a hereditary sensory and autonomic neuropathy, is caused by missplicing of exon 20, resulting from an intronic mutation in the inhibitor of kappa light polypeptide gene enhancer in B cells, kinase complex-associated protein (IKBKAP) gene encoding IKK complex-associated protein (IKAP)/elongator protein 1 (ELP1). A newly established splicing reporter assay allowed us to visualize pathogenic splicing in cells and to screen small chemicals for the ability to correct the aberrant splicing of IKBKAP. Using this splicing reporter, we screened our chemical libraries and ide

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15

Schäck, Manfred A., Kim Philipp Jablonski, Stefan Gräf, et al. "Eukaryotic life without tQCUG: the role of Elongator-dependent tRNA modifications in Dictyostelium discoideum." Nucleic Acids Research 48, no. 14 (2020): 7899–913. http://dx.doi.org/10.1093/nar/gkaa560.

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Abstract In the Elongator-dependent modification pathway, chemical modifications are introduced at the wobble uridines at position 34 in transfer RNAs (tRNAs), which serve to optimize codon translation rates. Here, we show that this three-step modification pathway exists in Dictyostelium discoideum, model of the evolutionary superfamily Amoebozoa. Not only are previously established modifications observable by mass spectrometry in strains with the most conserved genes of each step deleted, but also additional modifications are detected, indicating a certain plasticity of the pathway in the amo

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16

Rapino, Francesca, and Pierre Close. "Wobble uridine tRNA modification: a new vulnerability of refractory melanoma." Molecular & Cellular Oncology 5, no. 6 (2018): e1513725. http://dx.doi.org/10.1080/23723556.2018.1513725.

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17

Lin, Zhewang, Min Dong, Yugang Zhang, Eunyoung Alisa Lee, and Hening Lin. "Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification." Nature Chemical Biology 12, no. 12 (2016): 995–97. http://dx.doi.org/10.1038/nchembio.2190.

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18

HUANG, B. "An early step in wobble uridine tRNA modification requires the Elongator complex." RNA 11, no. 4 (2005): 424–36. http://dx.doi.org/10.1261/rna.7247705.

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19

Hermand, Damien. "Anticodon Wobble Uridine Modification by Elongator at the Crossroad of Cell Signaling, Differentiation, and Diseases." Epigenomes 4, no. 2 (2020): 7. http://dx.doi.org/10.3390/epigenomes4020007.

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First identified 20 years ago as an RNA polymerase II-associated putative histone acetyltransferase, the conserved Elongator complex has since been recognized as the central player of a complex, regulated, and biologically relevant epitranscriptomic pathway targeting the wobble uridine of some tRNAs. Numerous studies have contributed to three emerging concepts resulting from anticodon modification by Elongator: the codon-specific control of translation, the ability of reprogramming translation in various physiological or pathological contexts, and the maintenance of proteome integrity by count

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20

Scheidt, Viktor, Andre Juedes, Christian Baer, Roland Klassen, and Raffael Schaffrath. "Loss of wobble uridine modification in tRNA anticodons interferes with TOR pathway signaling." Microbial Cell 1, no. 12 (2014): 416–24. http://dx.doi.org/10.15698/mic2014.12.179.

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21

Selvadurai, Kiruthika, Pei Wang, Joseph Seimetz, and Raven H. Huang. "Archaeal Elp3 catalyzes tRNA wobble uridine modification at C5 via a radical mechanism." Nature Chemical Biology 10, no. 10 (2014): 810–12. http://dx.doi.org/10.1038/nchembio.1610.

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22

Mehlgarten, Constance, Daniel Jablonowski, Uta Wrackmeyer, et al. "Elongator function in tRNA wobble uridine modification is conserved between yeast and plants." Molecular Microbiology 76, no. 5 (2010): 1082–94. http://dx.doi.org/10.1111/j.1365-2958.2010.07163.x.

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23

Mehlgarten, Constance, Daniel Jablonowski, Uta Wrackmeyer, et al. "Elongator function in tRNA wobble uridine modification is conserved between yeast and plants." Molecular Microbiology 77, no. 2 (2010): 531. http://dx.doi.org/10.1111/j.1365-2958.2010.07253.x.

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24

Kurata, S., T. Ohtsuki, T. Wada, et al. "Decoding property of C5 uridine modification at the wobble position of tRNA anticodon." Nucleic Acids Symposium Series 3, no. 1 (2003): 245–46. http://dx.doi.org/10.1093/nass/3.1.245.

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25

Jeong, Sehwang, and Jungwook Kim. "Structural snapshots of CmoB in various states during wobble uridine modification of tRNA." Biochemical and Biophysical Research Communications 534 (January 2021): 604–9. http://dx.doi.org/10.1016/j.bbrc.2020.11.033.

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26

Abbassi, Nour-el-Hana, Anna Biela, Sebastian Glatt, and Ting-Yu Lin. "How Elongator Acetylates tRNA Bases." International Journal of Molecular Sciences 21, no. 21 (2020): 8209. http://dx.doi.org/10.3390/ijms21218209.

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Elp3, the catalytic subunit of the eukaryotic Elongator complex, is a lysine acetyltransferase that acetylates the C5 position of wobble-base uridines (U34) in transfer RNAs (tRNAs). This Elongator-dependent RNA acetylation of anticodon bases affects the ribosomal translation elongation rates and directly links acetyl-CoA metabolism to both protein synthesis rates and the proteome integrity. Of note, several human diseases, including various cancers and neurodegenerative disorders, correlate with the dysregulation of Elongator’s tRNA modification activity. In this review, we focus on recent fi

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27

Monies, Dorota, Cathrine Broberg Vågbø, Mohammad Al-Owain, Suzan Alhomaidi, and Fowzan S. Alkuraya. "Recessive Truncating Mutations in ALKBH8 Cause Intellectual Disability and Severe Impairment of Wobble Uridine Modification." American Journal of Human Genetics 104, no. 6 (2019): 1202–9. http://dx.doi.org/10.1016/j.ajhg.2019.03.026.

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28

Armengod, M. Eugenia, Salvador Meseguer, Magda Villarroya, et al. "Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes." RNA Biology 11, no. 12 (2014): 1495–507. http://dx.doi.org/10.4161/15476286.2014.992269.

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29

Chen, Changchun, Bo Huang, Mattias Eliasson, Patrik Rydén, and Anders S. Byström. "Elongator Complex Influences Telomeric Gene Silencing and DNA Damage Response by Its Role in Wobble Uridine tRNA Modification." PLoS Genetics 7, no. 9 (2011): e1002258. http://dx.doi.org/10.1371/journal.pgen.1002258.

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30

Moukadiri, Ismaïl, M. José Garzón, Glenn R. Björk, and M. Eugenia Armengod. "The output of the tRNA modification pathways controlled by the Escherichia coli MnmEG and MnmC enzymes depends on the growth conditions and the tRNA species." Nucleic Acids Research 42, no. 4 (2013): 2602–23. http://dx.doi.org/10.1093/nar/gkt1228.

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Abstract In Escherichia coli, the MnmEG complex modifies transfer RNAs (tRNAs) decoding NNA/NNG codons. MnmEG catalyzes two different modification reactions, which add an aminomethyl (nm) or carboxymethylaminomethyl (cmnm) group to position 5 of the anticodon wobble uridine using ammonium or glycine, respectively. In and , however, cmnm5 appears as the final modification, whereas in the remaining tRNAs, the MnmEG products are converted into 5-methylaminomethyl (mnm5) through the two-domain, bi-functional enzyme MnmC. MnmC(o) transforms cmnm5 into nm5, whereas MnmC(m) converts nm5 into mnm5, th

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31

Leszczynska, Grazyna, Marek Cypryk, Bartlomiej Gostynski, et al. "C5-Substituted 2-Selenouridines Ensure Efficient Base Pairing with Guanosine; Consequences for Reading the NNG-3′ Synonymous mRNA Codons." International Journal of Molecular Sciences 21, no. 8 (2020): 2882. http://dx.doi.org/10.3390/ijms21082882.

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5-Substituted 2-selenouridines (R5Se2U) are post-transcriptional modifications present in the first anticodon position of transfer RNA. Their functional role in the regulation of gene expression is elusive. Here, we present efficient syntheses of 5-methylaminomethyl-2-selenouridine (1, mnm5Se2U), 5-carboxymethylaminomethyl-2-selenouridine (2, cmnm5Se2U), and Se2U (3) alongside the crystal structure of the latter nucleoside. By using pH-dependent potentiometric titration, pKa values for the N3H groups of 1–3 were assessed to be significantly lower compared to their 2-thio- and 2-oxo-congeners.

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32

Xu, Fu, Anders S. Byström, and Marcus J. O. Johansson. "SSD1 modifies phenotypes of Elongator mutants." Current Genetics 66, no. 3 (2019): 481–85. http://dx.doi.org/10.1007/s00294-019-01048-9.

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AbstractThe translational decoding properties of tRNAs are influenced by post-transcriptional modification of nucleosides in their anticodon region. The Elongator complex promotes the first step in the formation of 5-methoxycarbonylmethyl (mcm5), 5-methoxycarbonylhydroxymethyl (mchm5), and 5-carbamoylmethyl (ncm5) groups on wobble uridine residues in eukaryotic cytosolic tRNAs. Elongator mutants in yeast, worms, plants, mice, and humans not only show a tRNA modification defect, but also a diverse range of additional phenotypes. Even though the phenotypes are almost certainly caused by the redu

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33

Takai, Kazuyuki, Shuhei Okumura, Kazumi Hosono, Shigeyuki Yokoyama, and Hiroshi Takaku. "A single uridine modification at the wobble position of an artificial tRNA enhances wobbling in an Escherichia coli cell-free translation system." FEBS Letters 447, no. 1 (1999): 1–4. http://dx.doi.org/10.1016/s0014-5793(99)00255-0.

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34

Lauhon, Charles T. "Identification and Characterization of Genes Required for 5-Hydroxyuridine Synthesis in Bacillus subtilis and Escherichia coli tRNA." Journal of Bacteriology 201, no. 20 (2019). http://dx.doi.org/10.1128/jb.00433-19.

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ABSTRACT In bacteria, tRNAs that decode 4-fold degenerate family codons and have uridine at position 34 of the anticodon are typically modified with either 5-methoxyuridine (mo5U) or 5-methoxycarbonylmethoxyuridine (mcmo5U). These modifications are critical for extended recognition of some codons at the wobble position. Whereas the alkylation steps of these modifications have been described, genes required for the hydroxylation of U34 to give 5-hydroxyuridine (ho5U) remain unknown. Here, a number of genes in Escherichia coli and Bacillus subtilis are identified that are required for wild-type

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35

Rosu, Adeline, Najla El Hachem, Francesca Rapino, et al. "Loss of tRNA-modifying enzyme Elp3 activates a p53-dependent antitumor checkpoint in hematopoiesis." Journal of Experimental Medicine 218, no. 3 (2021). http://dx.doi.org/10.1084/jem.20200662.

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The hematopoietic system is highly sensitive to perturbations in the translational machinery, of which an emerging level of regulation lies in the epitranscriptomic modification of transfer RNAs (tRNAs). Here, we interrogate the role of tRNA anticodon modifications in hematopoiesis by using mouse models of conditional inactivation of Elp3, the catalytic subunit of Elongator that modifies wobble uridine in specific tRNAs. Loss of Elp3 causes bone marrow failure by inducing death in committing progenitors and compromises the grafting activity of hematopoietic stem cells. Mechanistically, Elp3 de

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36

Rapino, Francesca, Zhaoli Zhou, Ana Maria Roncero Sanchez, et al. "Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate." Nature Communications 12, no. 1 (2021). http://dx.doi.org/10.1038/s41467-021-22254-5.

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AbstractRegulation of mRNA translation elongation impacts nascent protein synthesis and integrity and plays a critical role in disease establishment. Here, we investigate features linking regulation of codon-dependent translation elongation to protein expression and homeostasis. Using knockdown models of enzymes that catalyze the mcm5s2 wobble uridine tRNA modification (U34-enzymes), we show that gene codon content is necessary but not sufficient to predict protein fate. While translation defects upon perturbation of U34-enzymes are strictly dependent on codon content, the consequences on prot

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37

Xu, Sunwang, Ming Zhan, Cen Jiang, et al. "Genome-wide CRISPR screen identifies ELP5 as a determinant of gemcitabine sensitivity in gallbladder cancer." Nature Communications 10, no. 1 (2019). http://dx.doi.org/10.1038/s41467-019-13420-x.

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AbstractGemcitabine is the first-line treatment for locally advanced and metastatic gallbladder cancer (GBC), but poor gemcitabine response is universal. Here, we utilize a genome-wide CRISPR screen to identify that loss of ELP5 reduces the gemcitabine-induced apoptosis in GBC cells in a P53-dependent manner through the Elongator complex and other uridine 34 (U34) tRNA-modifying enzymes. Mechanistically, loss of ELP5 impairs the integrity and stability of the Elongator complex to abrogate wobble U34 tRNA modification, and directly impedes the wobble U34 modification-dependent translation of hn

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38

Gao, Ting, Fangyan Yuan, Zewen Liu, et al. "Proteomic and Metabolomic Analyses Provide Insights into the Mechanism on Arginine Metabolism Regulated by tRNA Modification Enzymes GidA and MnmE of Streptococcus suis." Frontiers in Cellular and Infection Microbiology 10 (December 11, 2020). http://dx.doi.org/10.3389/fcimb.2020.597408.

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GidA and MnmE, two important tRNA modification enzymes, are contributed to the addition of the carboxymethylaminomethyl (cmnm) group onto wobble uridine of tRNA. GidA-MnmE modification pathway is evolutionarily conserved among Bacteria and Eukarya, which is crucial in efficient and accurate protein translation. However, its function remains poorly elucidated in zoonotic Streptococcus suis (SS). Here, a gidA and mnmE double knock-out (DKO) strain was constructed to systematically decode regulatory characteristics of GidA-MnmE pathway via proteomic. TMT labelled proteomics analysis identified th

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39

Keller, Christopher, Manas Chattopadhyay, and Herbert Tabor. "Absolute requirement for polyamines for growth of Escherichia coli mutants (mnmE/G) defective in modification of the wobble anticodon of transfer-RNA." FEMS Microbiology Letters 366, no. 10 (2019). http://dx.doi.org/10.1093/femsle/fnz110.

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Abstract The genes mnmE and mnmG are responsible for the modification of uridine 34, ‘the wobble position’ of many aminoacyl-tRNAs. Deletion of these genes affects the strength of the codon-anticodon interactions of the aminoacyl-tRNAs with the mRNAs and the ribosomes. However, deletion of these genes does not usually have a significant effect on the growth rate of the standard Escherichia coli strains. In contrast, we have found that if the host E. coli strain is deficient in the synthesis of polyamines, deletion of the mnmE or mnmG gene results in complete inhibition of growth unless the med

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40

Laxman, Sunil, and Benjamin P. Tu. "tRNA wobble‐uridine modification pathways play critical roles in maintaining growth under nutrient limitation by altering the translational capacity of the cell." FASEB Journal 26, S1 (2012). http://dx.doi.org/10.1096/fasebj.26.1_supplement.944.2.

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41

Hepowit, Nathaniel L., and Julie A. Maupin-Furlow. "Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea." Journal of Bacteriology 201, no. 15 (2019). http://dx.doi.org/10.1128/jb.00254-19.

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ABSTRACT Ubiquitin-like protein (Ubl) modification targets proteins for transient inactivation and/or proteasome-mediated degradation in archaea. Here the rhodanese-like domain (RHD) protein UbaC (HVO_1947) was found to copurify with the E1-like enzyme (UbaA) of the Ubl modification machinery in the archaeon Haloferax volcanii. UbaC was shown to be important for Ubl ligation, particularly for the attachment of the Ubl SAMP2/3s to protein targets after exposure to oxidants (NaOCl, dimethyl sulfoxide [DMSO], and methionine sulfoxide [MetO]) and the proteasome inhibitor bortezomib. While UbaC was

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