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  • 1
    Electronic Resource
    Electronic Resource
    Phylogenetic relationship of ubiquitin repeats in the polyubiquitin gene from the marine sponge Geodia cydonium (1994)
    Springer
    Journal of molecular evolution 39 (1994), S. 369-377 
    Details
    ISSN: 1432-1432
    Keywords: Ubiquitin ; Phylogeny ; Sponges ; Geodia cydonium ; Evolution strategy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Ubiquitin is a 76-residue protein which is highly conserved among eukaryotes. Sponge (Porifera) ubiquitin, isolated from Geodia cydonium, is encoded by a gene (termed GCUBI) with six repeats, GCUBI-1 to GCUBI-6. All repeat units encode the same protein (with one exception: GCUBI-4 encodes ubiquitin with a change of Leu to Val at position 71). On the nt level the sequences of the six repeats differ considerably. All changes (except in GCUBI-4) are silent substitutions, which do not affect the protein structure. However, there is one major difference between the repeats: Codons from both codon families (TCN and AGPy) are simultaneously used for the serine at position 65. Using this characteristic the repeats were divided into two groups: Group I: GCUBI-1,3 (TCT codon) and GCUBI-5 (TCC); Group II: GCUBI-2,4,6 (AGC codon). Mutational analysis suggests that the sponge polyubiquitin gene evolved from an ancestral monoubiquitin gene by gene duplication and successive tandem duplications. The ancestral monoubiquitin gene most probably coded for threonine (ACC) at position 65. The first event, duplication of the monoubiquitin gene, happened some 110 million years ago. Since sponges from the genus Geodia are known from the Cretaceous (145 million) to recent time, it is very likely that all events in the evolution of polyubiquitin gene occurred in the same genus. Alignment data of the “consensus” ubiquitin nt sequences of different animals (man to protozoa) reflect very well the established phylogenetic relationships of the chosen organisms and show that the sponge ubiquitin gene branched off first from the multicellular organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00160269
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular evolution of the Metazoan protein kinase C multigene family (1996)
    Springer
    Journal of molecular evolution 43 (1996), S. 374-383 
    Details
    ISSN: 1432-1432
    Keywords: Sponges ; Geodia cydonium ; Serine/threonine kinases ; Phylogeny ; Molecular systematics ; Molecular evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protein kinases C (PKCs) comprise closely related Ser/Thr kinases, ubiquitously present in animal tissues; they respond to second messengers, e.g., Ca2+ and/or diacylglycerol, to express their activities. Two PKCs have been sequenced fromGeodia cydonium, a member of the lowest multicellular animals, the sponges (Porifera). One spongeG. cydonium PKC, GCPKC1, belongs to the “novel” (Ca2+-independent) PKC (nPKC) subfamily while the second one, GCPKC2, has the hallmarks of the “conventional” (Ca2+-dependent) PKC (cPKC) subfamily. The alignment of the Ser/Thr catalytic kinase domains, of the predicted as sequences for these cDNAs with respective segments from previously reported sequences, revealed highest homology to PKCs from animals but also distant relationships to Ser/Thr kinases from protozoa, plants, and bacteria. However, a comparison of the complete structures of the sponge PKCs, which are-already-identical to those of nPKCs and cPKCs from higher metazoa, with the structures of protozoan, plant, and bacterial Ser/Thr kinases indicates that the metazoan PKCs have to be distinguished from the nonmetazoan enzymes. These data indicate that metazoan PKCs have a universal common ancestor which they share with the nonmetazoan Ser/Thr kinases with respect to the kinase domain, but they differ from them in overall structural composition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02339011
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  • 3
    Electronic Resource
    Electronic Resource
    Sponge aggregation factor: In situ localization by fluorescent monoclonal antibody techniques (1986)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 31 (1986), S. 251-258 
    Details
    ISSN: 0730-2312
    Keywords: aggregation factor ; monoclonal antibodies ; reaggregation ; cell recognition ; Geodia cydonium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The aggregation factor (AF) from sponges mediates a heterophilic interaction of homologous cells. Applying electron microscopical means, we succeeded only very rarely in identifying the 90 S AF particle in tissue sections from Geodia cydonium. By means of a fluorescent antibody technique, we have now localized the cell binding domain of the AF in situ. Previous studies in this laboratory have led to the identification of the 47-kDa cell binding protein of the AF, using the monoclonal antibody (mab) 5D2-D11 [Gramzow M, Bachmann M, Zahn RK, Uhlenbruck G, Dorn A, Müller WEG, J Cell Biol, 102:1344-1349, 1986]. This mab and mab 7D5, directed against a 92-kDa protein in the AF complex, were chosen for the fluorescent studies. By using mab 5D2-D11, the plasma membranes of cells from different regions in the sponge could be brightly stained. However, mab 7D5 reacted only very weakly with the sponge surfaces. By applying the immuno-blotting technique it was furthermore demonstrated that the cell binding protein is present both in the associated form with AF complex and in a free state. Moreover, it was established that the 47-kDa binding protein is not present in (1) homologous glycoconjugates, (2) lectin, or (3) collagen; these components are known to be involved in cell-matrix interaction.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240310402
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