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Query: UNIPROT:P62988 (Ubiquitin)
 4,326 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The expression of the polyubiquitin-encoding gene (ubq-1) of Caenorhabditis elegans was analysed using transgenic nematode lines carrying translational ubq-1::lacZ fusions. Animals carrying a construct consisting of 938 bp of ubq-1 upstream sequences fused to lacZ (ubq938::lacZ) expressed beta Gal in embryos and in a tissue-general manner in 20% of L1 larvae. Somatic expression in later stages was usually confined to body muscle. Progressively larger deletions extending from the 5' end of ubq938::lacZ did not significantly alter the pattern of expression until 827 bp of sequence had been removed. Thus, sequences upstream from the transcription start point, including a G+C-rich block and a sequence resembling a TATA box (GAATAA), are not required to generate the expression pattern seen with ubq938::lacZ. Moreover, a basal level of expression was maintained in embryos when 903 bp were deleted. These results suggest that the promoter elements required for efficient expression of ubq-1 may reside within the transcribed region of the gene; alternatively, they must lie more than 1.7 kb upstream or 0.8 kb downstream from this region. Polymerase chain reaction analysis indicates that RNA molecules transcribed from the ubq938::lacZ and ubq delta 827::lacZ transgenes are trans-spliced to SL1, as is ubq-1 RNA.
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PMID:Expression of the polyubiquitin-encoding gene (ubq-1) in transgenic Caenorhabditis elegans. 131 99

The fau gene is the cellular homolog of the fox sequence in the Finkel-Biskis-Reilly Murine Sarcoma Virus (FBR-MuSV). This virus acquired the fau sequence in its reversed transcriptional orientation. Human and mouse fau cDNA's were identified and both encode a new protein of 133 AA. We show that fau (for FBR-MuSV associated ubiquitiously expressed gene) becomes expressed in all different tissues tested as a 600 bp messenger and we report the genomic structure of the human fau gene. The gene consists of five exons and four introns and the 5' untranslated region displays characteristic features for a housekeeping gene. Fau encodes the ribosomal protein S30 fused to a Ubiquitin-like protein.
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PMID:Genomic structure and expression of the human fau gene: encoding the ribosomal protein S30 fused to a ubiquitin-like protein. 132 60

The stress-induced expression of four different ubiquitin-encoding cDNAs was characterized in potato tuber tissue. The four clones exhibited differences in both structure and expression. The first cDNA encoded a single ubiquitin unit fused to an 80 amino acid ribosomal extension protein identical to the extension protein from tomato. Accumulation of the fusion transcript was induced by injury or ethylene, but not by heat shock. The three remaining ubiquitin cDNAs encoded polyubiquitins with 6 to 7 ubiquitin repeats. The first polyubiquitin gene was induced by injury, heat, or ethylene treatments. The second was induced also by injury or heat, with limited ethylene-dependent accumulation of transcript. Transcript levels of the third polyubiquitin gene were highest in control tubers and decreased markedly with injury, heat shock, or ethylene treatment. The data demonstrate the independent regulation of the different members of the ubiquitin gene family in response to stress and exogenous ethylene.
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PMID:Expression of stress-responsive ubiquitin genes in potato tubers. 132 70

Ubiquitin belongs to a multigene family. In Drosophila two members of this family have been previously described. We report here the organization and expression of a third member, the DUb52 gene, isolated by screening a Drosophila melanogaster genomic library. This gene encodes an ubiquitin monomer fused to a 52-amino acid extension protein. There are no introns interrupting the coding sequence. Recently, it has been described that this extension encodes a ribosomal protein in Saccharomyces, Dictyostelium, and Arabidopsis. The present results show that the 5' regulatory region of DUb52 shares common features with the ribosomal protein genes of Drosophila, Xenopus and mouse, including GC- and pyrimidine-rich regions. Moreover, sequences similar to the consensus Ribo-box in Neurospora crassa have been identified. Furthermore, a sequence has been found that is similar to the binding site for the TFIIIA distal element factor from Xenopus laevis. The DUb52 gene is transcribed to a 0.9 kb mRNA that is expressed constitutively throughout development and is particularly abundant in ovaries. In addition, the DUb52 gene has been found to be preferentially transcribed in exponentially growing Drosophila cells.
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PMID:Structure and expression of the Drosophila ubiquitin-52-amino-acid fusion-protein gene. 138 84

The hypotrichous ciliate, Euplotes eurystomus, contains both a transcriptionally inactive micronucleus (MIC) and a transcriptionally active macronucleus (MAC) in the same cell. MAC DNA is small (0.5-20 kb), linear and highly amplified. Each DNA fragment consists of two telomeres, a single coding region, and the necessary control elements to regulate gene transcription and replication. The polyubiquitin gene consists of 898 bp, plus 28 bp of double-stranded and 14 bases of single-stranded DNA of the telomeric repeat G4T4 at each end. The coding region exists as three copies of the ubiquitin gene (690 bp) fused in a head-to-tail arrangement as in other organisms. The stop codon is TAA, as in other Euplotes genes, and is not the rare glutamine codon used in most other ciliates. The 3' nontranslated region contains two presumptive poly(A) addition sites; the 5' nontranslated region possesses two putative TATA boxes, several imperfect direct and inverted repeats, and a possible origin of replication. Nucleosome positioning studies reveal four tightly packed nucleosomes and a non-nucleosomal area containing the probable 5' control region as well as part of the coding region. The 5' area does not contain any DNAse I hypersensitive sites. Although the telomeres are protected from exonuclease digestion, they are not as well protected as Oxytricha telomeres against endonucleases and cleavage by methidium propyl Fe2+ EDTA.
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PMID:Structure of the macronuclear polyubiquitin gene in Euplotes. 165 39

Ubiquitin is ubiquitous in all eukaryotes and its amino acid sequence shows extreme conservation. Ubiquitin genes comprise direct repeats of the ubiquitin coding unit with no spacers. The nucleotide sequences coding for 13 ubiquitin genes from 11 species reported so far have been compiled and analyzed. The G + C content of codon third base reveals a positive linear correlation with the genome G + C content of the corresponding species. The slope strongly suggests that the overall G + C content of codons of polyubiquitin genes clearly reflects the genome G + C content by AT/GC substitutions at the codon third position. The G + C content of ubiquitin codon third base also shows a positive linear correlation with the overall G + C content of coding regions of compiled genes, indicating the codon choices among synonymous codons reflect the average codon usage pattern of corresponding species. On the other hand, the monoubiquitin gene, which is different from the polyubiquitin gene in gene organization, gene expression, and function of the encoding protein, shows a different codon usage pattern compared with that of the polyubiquitin gene. From comparisons of the levels of synonymous substitutions among ubiquitin repeats and the homology of the amino acid sequence of the tail of monomeric ubiquitin genes, we propose that the molecular evolution of ubiquitin genes occurred as follows: Plural primitive ubiquitin sequences were dispersed on genome in ancestral eukaryotes. Some of them situated in a particular environment fused with the tail sequence to produce monomeric ubiquitin genes that were maintained across species. After divergence of species, polyubiquitin genes were formed by duplication of the other primitive ubiquitin sequences on different chromosomes. Differences in the environments in which ubiquitin genes are embedded reflect the differences in codon choice and in gene expression pattern between poly- and monomeric ubiquitin genes.
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PMID:Essential factors determining codon usage in ubiquitin genes. 166 81

We isolated and characterized two related ubiquitin genes from Drosophila melanogaster, polyubiquitin and UB3-D. The polyubiquitin gene contained 18 repeats of the 228-base-pair monomeric ubiquitin-encoding unit arranged in tandem. This gene was localized to a minor heat shock puff site, 63F, and it encoded a constitutively expressed 4.4-kilobase polyubiquitin-encoding mRNA, whose level was induced threefold by heat shock. To investigate the pattern of expression of the polyubiquitin gene in developing animals, a polyubiquitin-lacZ fusion gene was introduced into the Drosophila genome by germ line transformation. The fusion gene was expressed at high levels in a tissue-general manner at all life stages assayed. The ubiquitin-encoding gene, UB3-D, consisted of one ubiquitin-encoding unit directly fused, in frame, to a nonhomologous tail sequence. The amino acid sequence of the tail portion of the protein had 65% positional identity with that of yeast UBI3 protein, including a region that contained a potential nucleic acid-binding motif. The Drosophila UB3-D gene hybridized to a 0.9-kilobase mRNA that was constitutively expressed, and in contrast to the polyubiquitin gene, it was not inducible by heat shock.
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PMID:Structure and expression of ubiquitin genes of Drosophila melanogaster. 246 65

We have cloned and sequenced a polyubiquitin gene from Neurospora crassa that is organized in a four repeat-tandem array. The first repeat contains a small intron and the last is fused to an extra glutamine codon. In Northern blots, two RNA species of 1.3 kb and 0.7 kb hybridize to the isolated clone. The larger ubiquitin (UBI) transcript accumulates after partial inhibition of protein synthesis with cycloheximide, and the smaller one preferentially accumulates in conidia after germination. Unexpectedly, constitutive expression of UBI transcripts in exponentially grown mycelia is not altered by heat-shock or exposure to arsenite.
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PMID:Ubiquitin expression in Neurospora crassa: cloning and sequencing of a polyubiquitin gene. 254 9

In eukaryotic cells ubiquitin is synthesized as a polyubiquitin protein or as a protein fused at the carboxyl terminus to other polypeptides. An enzyme activity, ubiquitin protein peptidase, has been proposed to process these precursors by cleaving the peptide bond between adjoining ubiquitin molecules or between ubiquitin and the fused peptides. Using the cleavage of a 35S-labeled yeast ubiquitin protein fused to a synthetic 38-residue peptide obtained by in vivo metabolic labeling in Escherichia coli in an expression system based on the interaction of bacteriophage T7 RNA polymerase and its promoter, it is possible to detect a processing activity in soluble yeast extract. The specificity of the cleavage suggests this activity could be the in vivo processing activity for various ubiquitin precursor proteins in yeast cells. A similarly labeled ubiquitin protein fused to one cysteine residue was also utilized to detect an activity capable of removing a single cysteine residue from ubiquitin in a soluble extract. Employing assays based on the cleavage of labeled ubiquitin protein fusions, a ubiquitin protein peptidase activity from Saccharomyces cerevisiae was purified about 15,000-fold to yield a protein mixture consisting of only a few protein species. The major protein band which comigrated with the activities in in vitro assays has an apparent molecular weight of 29,000 when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two other protein species, about 20,000 and 10,000 in molecular weight, also comigrated with the in vitro activities throughout the purification procedure. Though our most purified protein fraction was shown to cleave various artificial ubiquitin protein fusions under our experimental conditions, it cannot cleave a ubiquitin dimer protein, suggesting the existence of functionally distinct ubiquitin protein peptidases. Our experimental protocol for preparing various labeled ubiquitin protein precursors provides a means to explore various processing enzymes existing in cells. The same protocol may also be adapted to prepare substrates for the study of other specific protein processing enzymes.
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PMID:Purification of a ubiquitin protein peptidase from yeast with efficient in vitro assays. 255 55

Ubiquitin, a highly conserved protein of 76 amino acids found in all eukaryotes, is translated from mRNAs that contain either multiple, contiguous coding sequences of the protein or a single ubiquitin coding sequence fused to sequences coding for 52 or 76 amino acids. We describe here formation of monoubiquitin from in vitro translation of mRNAs containing either two complete sequences or one complete ubiquitin and 60% of a second ubiquitin. No diubiquitin precursor was found with the complete diubiquitin mRNA, but the truncated mRNA formed proteins with apparent molecular masses of 30, 24, 7, and 4 kDa. The latter two are the expected products from truncated ubiquitin mRNA. The 30-kDa protein was immunoprecipitated by anti-ubiquitin antibodies and was converted to ubiquitin and the 4-kDa form by a ubiquitin isopeptidase-like activity in wheat germ. Other data indicated that the 30-kDa protein had multiple ubiquitins, all linked by isopeptide bonds to the truncated ubiquitin. One of these was the radiolabeled translation product, which should have been linked to the truncated protein by a normal peptide bond. A model is proposed in which ubiquitin itself participates in a transpeptidase activity.
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PMID:In vitro proteolytic processing of a diubiquitin and a truncated diubiquitin formed from in vitro-generated mRNAs. 283 55


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