Evolution and expression analysis of the sorghum ubiquitin-conjugating enzyme family

2019 ◽  
Vol 46 (3) ◽  
pp. 236
Author(s):  
Liqiang Jia ◽  
QiuFang Zhao ◽  
Shu Chen
Keyword(s):  
Current Knowledge ◽  
Functional Divergence ◽  
Signalling Pathways ◽  
E3 Ligases ◽  
Ubiquitin Conjugating Enzyme ◽  
Multiple Treatments ◽  
Ubiquitin Conjugating Enzymes ◽  
Encoding Genes ◽  
Sorghum Bicolor L ◽  
Conjugating Enzyme

Ubiquitin-conjugating enzymes (UBCs), which catalyse the transfer of ubiquitin to substrate or E3 ligases, are key enzymes in ubiquitination modifications of target proteins. Current knowledge regarding the sorghum (Sorghum bicolor (L.) Moench) ubiquitin-conjugating enzyme (SbUBC) family remains very limited. We identified 53 UBC-encoding genes in the sorghum genome and divided these into 18 groups according to their phylogenetic relationship with Arabidopsis thaliana (L.) Heynh., which was further supported by conserved motif and gene structure analyses. Different expression levels under a variety of abiotic stresses suggested that these might participate in distinct signalling pathways and that they underwent functional divergence during evolution. Furthermore, several SbUBC genes responded to single treatments, and individual SbUBC genes responded to multiple treatments, suggesting that sorghum UBCs may mediate crosstalk among different signalling pathways. Overall, the results provide valuable information for better understanding the classification and putative functions of sorghum UBC-encoding genes.

scholarly journals Targeting neddylation E2s: a novel therapeutic strategy in cancer

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Yi-Chao Zheng ◽  
Yan-Jia Guo ◽  
Bo Wang ◽  
Chong Wang ◽  
M. A. A. Mamun ◽  
...  
Keyword(s):  
Posttranslational Modification ◽  
Therapeutic Strategy ◽  
Neural Precursor Cell ◽  
Catalytic Core Domain ◽  
Catalytic Core ◽  
Core Domain ◽  
E3 Ligases ◽  
Ubiquitin Conjugating Enzyme ◽  
E2 Enzymes ◽  
Conjugating Enzyme

AbstractUbiquitin-conjugating enzyme E2 M (UBE2M) and ubiquitin-conjugating enzyme E2 F (UBE2F) are the two NEDD8-conjugating enzymes of the neddylation pathway that take part in posttranslational modification and change the activity of target proteins. The activity of E2 enzymes requires both a 26-residue N-terminal docking peptide and a conserved E2 catalytic core domain, which is the basis for the transfer of neural precursor cell-expressed developmentally downregulated 8 (NEDD8). By recruiting E3 ligases and targeting cullin and non-cullin substrates, UBE2M and UBE2F play diverse biological roles. Currently, there are several inhibitors that target the UBE2M-defective in cullin neddylation protein 1 (DCN1) interaction to treat cancer. As described above, this review provides insights into the mechanism of UBE2M and UBE2F and emphasizes these two E2 enzymes as appealing therapeutic targets for the treatment of cancers.

scholarly journals OTUB1 non-catalytically stabilizes the E2 ubiquitin-conjugating enzyme UBE2E1 by preventing its autoubiquitination

2018 ◽  
Vol 293 (47) ◽  
pp. 18285-18295 ◽  
Author(s):  
Nagesh Pasupala ◽  
Marie E. Morrow ◽  
Lauren T. Que ◽  
Barbara A. Malynn ◽  
Averil Ma ◽  
...  
Keyword(s):  
Polyubiquitin Chains ◽  
Protein Ubiquitination ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzymes ◽  
E2 Enzymes ◽  
Ubiquitin Conjugating Enzymes ◽  
In Cells ◽  
Conjugating Enzyme

OTUB1 is a deubiquitinating enzyme that cleaves Lys-48–linked polyubiquitin chains and also regulates ubiquitin signaling through a unique, noncatalytic mechanism. OTUB1 binds to a subset of E2 ubiquitin-conjugating enzymes and inhibits their activity by trapping the E2∼ubiquitin thioester and preventing ubiquitin transfer. The same set of E2s stimulate the deubiquitinating activity of OTUB1 when the E2 is not charged with ubiquitin. Previous studies have shown that, in cells, OTUB1 binds to E2-conjugating enzymes of the UBE2D (UBCH5) and UBE2E families, as well as to UBE2N (UBC13). Cellular roles have been identified for the interaction of OTUB1 with UBE2N and members of the UBE2D family, but not for interactions with UBE2E E2 enzymes. We report here a novel role for OTUB1–E2 interactions in modulating E2 protein ubiquitination. We observe that Otub1−/− knockout mice exhibit late-stage embryonic lethality. We find that OTUB1 depletion dramatically destabilizes the E2-conjugating enzyme UBE2E1 (UBCH6) in both mouse and human OTUB1 knockout cell lines. Of note, this effect is independent of the catalytic activity of OTUB1, but depends on its ability to bind to UBE2E1. We show that OTUB1 suppresses UBE2E1 autoubiquitination in vitro and in cells, thereby preventing UBE2E1 from being targeted to the proteasome for degradation. Taken together, we provide evidence that OTUB1 rescues UBE2E1 from degradation in vivo.

scholarly journals Two Ubiquitin-Conjugating Enzymes, UbcP1/Ubc4 and UbcP4/Ubc11, Have Distinct Functions for Ubiquitination of Mitotic Cyclin

2003 ◽  
Vol 23 (10) ◽  
pp. 3497-3505 ◽  
Author(s):  
Hiroaki Seino ◽  
Tsutomu Kishi ◽  
Hideo Nishitani ◽  
Fumiaki Yamao
Keyword(s):  
Fission Yeast ◽  
Ubiquitin Proteasome System ◽  
High Expression ◽  
Mitotic Cyclin ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzymes ◽  
Ubiquitin Conjugating Enzymes ◽  
Mutant Cells ◽  
Conjugating Enzyme

ABSTRACT Cell cycle events are regulated by sequential activation and inactivation of Cdk kinases. Mitotic exit is accomplished by the inactivation of mitotic Cdk kinase, which is mainly achieved by degradation of cyclins. The ubiquitin-proteasome system is involved in this process, requiring APC/C (anaphase-promoting complex/cyclosome) as a ubiquitin ligase. In Xenopus and clam oocytes, the ubiquitin-conjugating enzymes that function with APC/C have been identified as two proteins, UBC4 and UBCx/E2-C. Previously we reported that the fission yeast ubiquitin-conjugating enzyme UbcP4/Ubc11, a homologue of UBCx/E2-C, is required for mitotic transition. Here we show that the other fission yeast ubiquitin-conjugating enzyme, UbcP1/Ubc4, which is homologous to UBC4, is also required for mitotic transition in the same manner as UbcP4/Ubc11. Both ubiquitin-conjugating enzymes are essential for cell division and directly required for the degradation of mitotic cyclin Cdc13. They function nonredundantly in the ubiquitination of CDC13 because a defect in ubcP1/ubc4 + cannot be suppressed by high expression of UbcP4/Ubc11 and a defect in ubcP4/ubc11 + cannot be suppressed by high expression of UbcP1/Ubc4. In vivo analysis of the ubiquitinated state of Cdc13 shows that the ubiquitin chains on Cdc13 were short in ubcP1/ubc4 mutant cells while ubiquitinated Cdc13 was totally reduced in ubcP4/ubc11 mutant cells. Taken together, these results indicate that the two ubiquitin-conjugating enzymes play distinct and essential roles in the degradation of mitotic cyclin Cdc13, with the UbcP4/Ubc11-pathway initiating ubiquitination of Cdc13 and the UbcP1/Ubc4-pathway elongating the short ubiquitin chains on Cdc13.

Hug and hold tight: Dimerization controls the turnover of the ubiquitin-conjugating enzyme UBE2S

2020 ◽  
Vol 13 (654) ◽  
pp. eabd9892
Author(s):  
Anja Bremm
Keyword(s):  
Half Life ◽  
Anaphase Promoting Complex ◽  
Ubiquitin Chain ◽  
Precise Control ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzymes ◽  
Chain Synthesis ◽  
Ubiquitin Conjugating Enzymes ◽  
Conjugating Enzyme

Precise control of the activity and abundance of ubiquitin-conjugating enzymes (E2s) ensures fidelity in ubiquitin chain synthesis. In this issue of Science Signaling, Liess et al. demonstrate that the human anaphase-promoting complex (APC/C)–associated E2 UBE2S adopts an autoinhibited dimeric state that increases the half-life of UBE2S by preventing its autoubiquitination-driven turnover.

scholarly journals RBR-Type E3 Ligases and the Ubiquitin-Conjugating Enzyme UBC26 Regulate Abscisic Acid Receptor Levels and Signaling

2019 ◽  
Vol 182 (4) ◽  
pp. 1723-1742 ◽  
Author(s):  
Maria Angeles Fernandez ◽  
Borja Belda-Palazon ◽  
Jose Julian ◽  
Alberto Coego ◽  
Jorge Lozano-Juste ◽  
...  
Keyword(s):  
Abscisic Acid ◽  
E3 Ligases ◽  
Acid Receptor ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme

scholarly journals Interaction with a Host Ubiquitin-Conjugating Enzyme Is Required for the Pathogenicity of a Geminiviral DNA β Satellite

2009 ◽  
Vol 22 (6) ◽  
pp. 737-746 ◽  
Author(s):  
Omid Eini ◽  
Satish Dogra ◽  
Luke A. Selth ◽  
Ian B. Dry ◽  
John W. Randles ◽  
...  
Keyword(s):  
Single Gene ◽  
Bimolecular Fluorescence Complementation ◽  
Cotton Leaf ◽  
Specific Symptom ◽  
Ubiquitin Conjugating Enzyme ◽  
Ubiquitin Proteasome ◽  
Ubiquitin Conjugating Enzymes ◽  
Conjugating Enzyme

DNA β is a single-stranded satellite DNA which encodes a single gene, βC1. To better understand the role of βC1 in the pathogenicity of DNA β, a yeast two-hybrid screen of a tomato cDNA library was carried out using βC1 from Cotton leaf curl Multan virus (CLCuMV) DNA β as the bait. A ubiquitin-conjugating enzyme, designated SlUBC3, which functionally complemented a yeast mutant deficient in ubiquitin-conjugating enzymes was identified. The authenticity and specificity of the interaction between βC1 and SlUBC3 was confirmed both in vivo, using a bimolecular fluorescence complementation assay, and in vitro, using a protein-binding assay. Analysis of deletion mutants of the βC1 protein showed that a myristoylation-like motif is required both for its interaction with SlUBC3 and the induction of DNA-β-specific symptoms in host plants. The level of polyubiquitinated proteins in transgenic tobacco plants expressing βC1 was found to be reduced compared with wild-type plants. These results are consistent with the hypothesis that interaction of βC1 with SlUBC3 is required for DNA-β-specific symptom induction, and that this is possibly due to downregulation of the host ubiquitin proteasome pathway.

scholarly journals A Giant Ubiquitin-conjugating Enzyme Related to IAP Apoptosis Inhibitors

1998 ◽  
Vol 141 (6) ◽  
pp. 1415-1422 ◽  
Author(s):  
Hans-Peter Hauser ◽  
Michael Bardroff ◽  
George Pyrowolakis ◽  
Stefan Jentsch
Keyword(s):  
Covalent Attachment ◽  
Protein Protein Interaction ◽  
Small Proteins ◽  
The Family ◽  
Golgi Compartment ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzymes ◽  
And Function ◽  
Ubiquitin Conjugating Enzymes ◽  
Conjugating Enzyme

Ubiquitin-conjugating enzymes (UBC) catalyze the covalent attachment of ubiquitin to target proteins and are distinguished by the presence of a UBC domain required for catalysis. Previously identified members of this enzyme family are small proteins and function primarily in selective proteolysis pathways. Here we describe BRUCE (BIR repeat containing ubiquitin-conjugating enzyme), a giant (528-kD) ubiquitin-conjugating enzyme from mice. BRUCE is membrane associated and localizes to the Golgi compartment and the vesicular system. Remarkably, in addition to being an active ubiquitin-conjugating enzyme, BRUCE bears a baculovirus inhibitor of apoptosis repeat (BIR) motif, which to this date has been exclusively found in apoptosis inhibitors of the IAP-related protein family. The BIR motifs of IAP proteins are indispensable for their anti–cell death activity and are thought to function through protein–protein interaction. This suggests that BRUCE may combine properties of IAP-like proteins and ubiquitin-conjugating enzymes and indicates that the family of IAP-like proteins is structurally and functionally more diverse than previously expected.

scholarly journals The Ubiquitin Conjugating Enzyme, UbcM2, Engages in Novel Interactions with Components of Cullin-3 Based E3 Ligases†

Biochemistry ◽  
2009 ◽  
Vol 48 (15) ◽  
pp. 3527-3537 ◽  
Author(s):  
Kendra S. Plafker ◽  
Jeffrey D. Singer ◽  
Scott M. Plafker
Keyword(s):  
E3 Ligases ◽  
Cullin 3 ◽  
Ubiquitin Conjugating Enzyme ◽  
Novel Interactions ◽  
Conjugating Enzyme

scholarly journals Distinct activation of an E2 ubiquitin-conjugating enzyme by its cognate E3 ligases

2015 ◽  
Vol 112 (7) ◽  
pp. E625-E632 ◽  
Author(s):  
Itamar Cohen ◽  
Reuven Wiener ◽  
Yuval Reiss ◽  
Tommer Ravid
Keyword(s):  
Transition State ◽  
Protein Quality ◽  
Noncovalent Interactions ◽  
Cellular Protein ◽  
Ring Domain ◽  
E3 Ligases ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme

A significant portion of ubiquitin (Ub)-dependent cellular protein quality control takes place at the endoplasmic reticulum (ER) in a process termed “ER-associated degradation” (ERAD). Yeast ERAD employs two integral ER membrane E3 Ub ligases: Hrd1 (also termed “Der3”) and Doa10, which recognize a distinct set of substrates. However, both E3s bind to and activate a common E2-conjugating enzyme, Ubc7. Here we describe a novel feature of the ERAD system that entails differential activation of Ubc7 by its cognate E3s. We found that residues within helix α2 of Ubc7 that interact with donor Ub were essential for polyUb conjugation. Mutagenesis of these residues inhibited the in vitro activity of Ubc7 by preventing the conjugation of donor Ub to the acceptor. Unexpectedly, Ub chain formation by mutant Ubc7 was restored selectively by the Hrd1 RING domain but not by the Doa10 RING domain. In agreement with the in vitro data, Ubc7 α2 helix mutations selectively impaired the in vivo degradation of Doa10 substrates but had no apparent effect on the degradation of Hrd1 substrates. To our knowledge, this is the first example of distinct activation requirements of a single E2 by two E3s. We propose a model in which the RING domain activates Ub transfer by stabilizing a transition state determined by noncovalent interactions between the α2 helix of Ubc7 and Ub and that this transition state may be stabilized further by some E3 ligases, such as Hrd1, through additional interactions outside the RING domain.

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