Cloning of a novel ubiquitin‐conjugating enzyme (E2) gene from the ciliate <i>Paramecium tetraurelia</i>

Okano, Satoshi; Tokushima, Hideyuki; Nakaoka, Yasuo; Shimizu, Kikuo

doi:10.1016/0014-5793(96)00689-8

Cited by 6 publications

(3 citation statements)

References 32 publications

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“…6 , Additional file 4 : Table S4 B/A) may be necessary for cells to survive at low temperature, or to enter a deeper level of dormancy. Of these, the highly expressed ribosomal protein L7 could be involved in the suppression of global protein synthesis and the cell cycle under cold conditions [ 41 ]; Bifunctional purine biosynthesis protein (putative) catalyzes the second and the fifth steps of de novo purine biosynthesis pathway [ 42 ]; Vacuolar ATP synthase in C. irritans theronts with higher expression might be involved in the process of host infection [ 2 ]; Heat shock protein 70 gene can improve protein folding together with some other chaperones [ 43 ]; 40S ribosomal protein S18 (putative) is involved in the initiation of translation [ 44 ]; Glutamine synthetaseis is involved in nitrogen metabolism, recycling of the neurotransmitter glutamate and glutamine biosynthesis for the production of amino acids, sugars, and glucosamine-6-phosphate [ 45 ]; Eukaryotic initiation factor 4A is a protein complex that mediates recruitment of ribosomes to mRNA [ 46 ] ; Ubiquitin-conjugating enzyme (putative) is involved in selective protein degradation, DNA repair, cell cycle control, and possibly the regulation of chromatin structure [ 47 ]. The mechanism of these DEGs still requires further investigation, e.g.…”

Section: Resultsmentioning

confidence: 99%

Transcriptome analysis of dormant tomonts of the marine fish ectoparasitic ciliate Cryptocaryon irritans under low temperature

et al. 2016

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BackgroundCryptocaryon irritans, a species of obligatory ciliate ectoparasite, can infect various species of marine teleost fish. Cryptocaryon irritans that fall to the seabed or aquarium bottom in winter can form “dormant tomonts” and wake up when the temperature rises the next year. Abundant studies and analyses on the dormant tomonts were carried out at the transcriptome level, in order to investigate the molecular mechanism of C. irritans tomonts entering the dormant state under low-temperature conditions.MethodsThe paired-end sequencing strategy was used to better assemble the entire transcriptome de novo. All clean sequencing reads from each of the three libraries (Group A: untreated blank control; Group B: treated for 24 h at 12 °C; and Group C: developed for 24 h at 25 °C) were respectively mapped back to the transcriptome assembly using the bioinformatics software.ResultsIn this study, 25,695,034, 21,944,467, and 28,722,875 paired-end clean reads were obtained respectively from the three cDNA libraries of the C. irritans tomont by Illumina paired-end sequencing technology. A total of 25,925 unique transcript fragments (unigenes) were assembled, with an average length of 839 bp. Differentially expressed genes (DEGs) were scrutinized; in Group B/A pairwise comparison, 343 genes presented differential expression, including 265 up-regulated genes and 78 down-regulated genes in Group B; in Group C/A pairwise comparison, there were 567 DEGs, including 548 up-regulated genes and 19 down-regulated genes in Group C; and in Group B/C pairwise comparison, 185 genes showed differential expression, including 145 up-regulated genes and 40 down-regulated genes in Group B.ConclusionsThis is the first transcriptomic analytical study of the C. irritans tomonts under low temperature. It can be concluded that most of the genes required for its cell survival under low temperature, or for cell entry into a deeper dormancy state were discovered, and that they might be considered as candidate genes to develop the diagnostic and control measures for cryptocaryoniasis.Electronic supplementary materialThe online version of this article (doi:10.1186/s13071-016-1550-1) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Transcriptome analysis of dormant tomonts of the marine fish ectoparasitic ciliate Cryptocaryon irritans under low temperature

et al. 2016

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“…E2s are structurally grouped into four classes [15], and class III E2s (UbcH6, UBE2E2, and UBE2E3) have N‐terminal extensions of various lengths, in addition to the well‐conserved UBC domains [16,17]. We have previously reported the molecular cloning of UBE2E2 [18] and UBE2E3 [19].…”

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confidence: 99%

N‐Terminally extended human ubiquitin‐conjugating enzymes (E2s) mediate the ubiquitination of RING‐finger proteins, ARA54 and RNF8

Ito

Adachi

Iwakami

et al. 2001

European Journal of Biochemistry

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We have previously cloned cDNAs encoding the N-terminally extended class III human ubiquitin-conjugating enzymes (E2s), UBE2E2 and UBE2E3, the biological functions of which are not known. In this study, we performed yeast twohybrid screening for protein(s) interacting with UBE2E2, and two RING-finger proteins, ARA54 and RNF8, were identified. Both ARA54, a ligand-dependent androgen receptor coactivator, and RNF8 interacted with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless) in the yeast two-hybrid assay. The use of various deletion mutants of UBE2E2 and RING-finger proteins and two RING point mutants, ARA54 C(220)S and RNF8 C(403)S, in which the RING structure is disrupted, showed that the UBC domain of UBE2E2 and the RING domain of these RING-finger proteins were involved in this association. Wild-type ARA54 and RNF8, expressed in insect Sf9 cells, catalyzed E2-dependent autoubiquitination in vitro, whereas the point mutated proteins showed markedly reduced activity. Ubiquitination of wild-type ARA54 and RNF8, expressed in COS-7 cells, was also observed, and a proteasome inhibitor, MG132, prevented the degradation of these wild-type proteins, but was much less effective in protecting the RING mutants. Transfection of COS-7 cells with a green fluorescent protein chimera showed that RNF8 was localized in the nucleus, and ARA54 in both the cytoplasm and nucleus. Our results suggest that ARA54 and RNF8 possibly act as Ub-ligases (E3) in the ubiquitination of certain nuclear protein(s).

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“…The active-site cysteine is underlined. tional C-terminal extensions (class II), that possesses additional N-terminal extensions (class III), and that possesses both Cand N-terminal extensions (class IV) (Matuschewski et al, 1996;Okano et al, 1996). Since UBE2E2 possesses an N-terminal extension in addition to the conserved UBC domain, this E2 is a member of class III enzymes such as human UbcH6, mouse UbcM2, mouse UbcM3 and Drosophila UbcD2.…”

Section: Figmentioning

confidence: 99%

cDNA cloning, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme

Kimura

Hattori

Matsuda

et al. 1997

Cytogenet Genome Res

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A cDNA encoding a human ubiquitin-conjugating enzyme (E2) with N-terminal extension (UBE2E2/UbcH8) was isolated. Amino acid sequence within the UBC domain of UBE2E2 shares over 90% identity with human UbcH6, mouse UbcM2, and Drosophila UbcD2, whereas the N-terminal region shows little amino acid sequence similarity with known proteins. The UBE2E2 gene is transcribed in various tissues as a 1.9-kb transcript. The UBE2E2 protein formed a thioester bond with ubiquitin in an E1-dependent manner, indicating that the gene product is a functional E2 enzyme. The UBE2E2 gene was assigned to human chromosome 3p24.2 by fluorescence in situ hybridization.

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Cloning of a novel ubiquitin‐conjugating enzyme (E2) gene from the ciliate Paramecium tetraurelia

Cited by 6 publications

References 32 publications

Transcriptome analysis of dormant tomonts of the marine fish ectoparasitic ciliate Cryptocaryon irritans under low temperature

Transcriptome analysis of dormant tomonts of the marine fish ectoparasitic ciliate Cryptocaryon irritans under low temperature

N‐Terminally extended human ubiquitin‐conjugating enzymes (E2s) mediate the ubiquitination of RING‐finger proteins, ARA54 and RNF8

cDNA cloning, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme

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