Complete cDNA sequence of a <i>Dictyostelium</i> ubiquitin with a carboxy‐terminal tail and identification of the protein using an anti‐peptide antibody

Müller‐Taubenberger, Annette; Westphal, Monika; Jaeger, Ernst; Noegel, Angelika A.; Gerisch, Günther

doi:10.1016/0014-5793(88)81139-6

Cited by 34 publications

(11 citation statements)

References 12 publications

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“…reinhardii, differs by one amino acid to the previously described ubiquitins from higher plants. The strongest divergence (three amino acid substitutions) from Chlumydomorrus ubiquitin (probably representing the largest evolutionary distance) is found in yeast [7] and D. discoideuni [39].…”

Section: Discussionmentioning

confidence: 99%

Ubiquitin in a lower plant

Pollmann

Kampen

Wettern

1991

European Journal of Biochemistry

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A detailed characterization of Chlamydomonas reinhardii cDNAs encoding ubiquitin 52‐amino‐acid fusion proteins is presented in this study. While two cDNAs (designated UBI1 and UBI3) encode the complete ubiquitin extension protein, the third one (UBI2) lacks a minor part of the 5′ region as well as a poly(A) tail. Differences between UBI1 and UBI3 are observed in the length of the poly(A) domain (13 versus 46 adenines) and in the lack of three nucleotides at the 3′ noncoding region of UBI3. According to Northern blot experiments using UBI1 as a homologous probe, at least six members of the C. reinhardii ubiquitin gene family are transcriptionally active at regular conditions. During application of severe stress (heat shock in light and darkness, and photoinhibition), the transcription of the UBI1 mRNA substantially decreases. This effect is most drastically induced by application of heat shock to illuminated cells.

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Section: Discussionmentioning

confidence: 99%

Ubiquitin in a lower plant

Pollmann

Kampen

Wettern

1991

European Journal of Biochemistry

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“…In addition, ubiquitination has been shown to be a component of the pathway by which the yeast MDR transporter Pdr5, the yeast ␣-factor receptor, and the mammalian growth hormone receptor are targeted for endocytosis (Egner and Kuchler, 1996;Hicke and Riezman, 1996;Strous et al, 1996), while ubiquitination/deubiquitination controls some cell fate decisions during development of the Drosophila eye (Jermyn and Williams, 1995) and larval development in Caenorhabditis elegans (Zhen et al, 1996). In Dictyostelium, the structure and regulation of expression of genes encoding ubiquitin have been examined (Muller-Taubenberger et al, 1988a and1988b;Ohmachi et al, 1989), and the in vitro ubiquitination and degradation of Dictyostelium calmodulin have been reported in a reticulocyte extract (Gregori et al, 1985). However, little is know about the role of protein ubiquitination during Dictyostelium development.…”

Section: Introductionmentioning

confidence: 99%

A Ubiquitin-Conjugating Enzyme Is Essential for Developmental Transitions inDictyostelium

Clark

Nomura

Mohanty

et al. 1997

MBoC

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We have identified a developmentally essential gene, UbcB, by insertional mutagenesis. The encoded protein (UBC1) shows very high amino acid sequence identity to ubiquitin-conjugating enzymes from other organisms, suggesting that UBC1 is involved in protein ubiquitination and possibly degradation during Dictyostelium development. Consistent with the homology of the UBC1 protein to UBCs, the developmental pattern of protein ubiquitination is altered in ubcB-null cells. ubcB-null cells are blocked in the ability to properly execute the developmental transition that occurs between the induction of postaggregative gene expression during mound formation and the induction of cell-type differentiation and subsequent morphogenesis. ubcB-null cells plated on agar form mounds with normal kinetics; however, they remain at this stage for ϳ10 h before forming multiple tips and fingers that then arrest. Under other conditions, some of the fingers form migrating slugs, but no culmination is observed. In ubcB-null cells, postaggregative gene transcripts accumulate to very high levels and do not decrease significantly with time as they do in wild-type cells. Expression of cell-type-specific genes is very delayed, with the level of prespore-specific gene expression being significantly reduced compared with that in wild-type cells. lacZ reporter studies using developmentally regulated and cell-type-specific promoters suggest that ubcB-null cells show an unusually elevated level of staining of lacZ reporters expressed in anterior-like cells, a regulatory cell population found scattered throughout the aggregate, and reduced staining of a prespore reporter. ubcB-null cells in a chimeric organism containing predominantly wildtype cells are able to undergo terminal differentiation but show altered spatial localization. In contrast, in chimeras containing only a small fraction of wild-type cells, the mature fruiting body is very small and composed almost exclusively of wild-type cells, with the ubcB-null cells being present as a mass of cells located in extreme posterior of the developing organism. The amino acid sequence analysis of the UbcB open reading frame (ORF) and the analysis of the developmental phenotypes suggest that tip formation and subsequent development requires specific protein ubiquitination, and possibly degradation. INTRODUCTIONA significant amount of information has been obtained about the signal transduction pathways that control many aspects of Dictyostelium differentiation (Devreotes, 1994;Firtel, 1995). Cyclic AMP, functioning as an extracellular ligand to a seven-span/serpentine class of receptors, mediates aggregation, the developmental switch to multicellular development, and celltype differentiation through distinct signal transduction pathways. Subsequent morphogenesis and the initiation of culmination are also believed to be regulated by cAMP functioning both as an extracellular signaling molecule and intracellularly through the activation of PKA (Williams and Morrison, 1994;Firtel, 1995). While both molecu...

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“…As shown in Fig. 6, the detected protein migrates well below the apparent molecular mass of 16-kDa for Ubex52 (44) and is not recognized by a polyclonal ubiquitin antibody (data not shown). This indicates that this protein represents the processed C-terminal extension of Ubex52, although others have detected predominantly the uncleaved form (45).…”

Section: Resultsmentioning

confidence: 97%

A Novel Component Involved in Ubiquitination Is Required for Development of Dictyostelium discoideum

Pukatzki

Tordilla

Franke

et al. 1998

Journal of Biological Chemistry

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A novel component of the ubiquitination system, called NOSA, is essential for cellular differentiation in Dictyostelium discoideum. Disruption of nosA does not affect the growth rate but causes an arrest in development after the cells have aggregated. nosA contains seven exons and codes for a developmentally regulated 3.5-kb mRNA. The 125-kDa NOSA protein is present in the cytosol at constant levels during growth and development. The C-terminal region of NOSA has homology with ubiquitin fusion degradation protein-2 (UFD2) of Saccharomyces cerevisiae and putative homologs in Caenorhabditis elegans and humans. UFD2 is involved in the ubiquitin-mediated degradation of model substrates in which ubiquitin forms part of the translation product, but ufd2 mutants have no detected phenotype. In accord with the homology to UFD2, we found differences in the ubiquitination patterns between nosA mutants and their parental cell line. While general in vivo and in vitro ubiquitination is minimally affected, ubiquitination of individual proteins is altered throughout growth and development in nosA mutants. These findings suggest that events involving ubiquitination are critical for progression through the aggregate stage of the Dictyostelium life cycle.Protein levels and activities are regulated by differential gene expression, translational regulation, and post-translational modification. One such modification is the attachment of the small 8-kDa ubiquitin protein to a specific set of substrates, which targets these proteins to proteasomes for degradation. Although the ubiquitin pathway has the capacity to degrade almost every protein, it is a benign component of the cytoplasm and the nucleus. The protein degradation cascade begins when ubiquitin is attached to ubiquitin-activating enzymes of the E1 1 class through a high energy thioester bond. Activated ubiquitin is then transferred to substrates by ubiquitin-conjugating enzymes of the E2 class. The carboxyl-terminal glycine of ubiquitin forms a covalent bond with the ⑀-NH 2 group of a lysine in the target protein. In some cases, the conjugation of ubiquitin to proteins also requires the E3 ubiquitin ligases, which form complexes with specific E2 conjugating enzymes and the substrate, to confer specificity. Subsequent cycles result in the formation of multimeric ubiquitin chains on the target protein that are recognized by the 19 S cap of the proteasome. The multiubiquitin chain is removed by ubiquitinspecific hydrolases before the protein is unfolded and enters the 20 S proteasome for degradation (see Ref.

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Complete cDNA sequence of a Dictyostelium ubiquitin with a carboxy‐terminal tail and identification of the protein using an anti‐peptide antibody

Cited by 34 publications

References 12 publications

Ubiquitin in a lower plant

Ubiquitin in a lower plant

A Ubiquitin-Conjugating Enzyme Is Essential for Developmental Transitions inDictyostelium

A Novel Component Involved in Ubiquitination Is Required for Development of Dictyostelium discoideum

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