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  • 1
    Electronic Resource
    Electronic Resource
    The β-1,6-glucan containing side-chain of cell wall proteins of Saccharomyces cerevisiae is bound to the glycan core of the GPI moiety (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 145 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Cell wall proteins of Saccharomyces cerevisiae are anchored by means of a β-1,6-glucan-containing side-chain. It is not known whether this chain is linked to the protein part (e.g. through carbohydrate side-chains) or to the glycosylphosphatidylinositol (GPI) moiety of cell wall proteins. An IgA protease recognition site was introduced in Cwp2p, a β-1,6-glucosylated cell wall protein, immediately N-terminal from the omega amino acid (the attachment site of the GPI moiety). Proteolytic cleavage of this site revealed that the β-1,6-glucan epitope was not linked to the protein part. We conclude that neither N- or O-glycosylation is involved in β-glucosylation of cell wall proteins. This confirms that the glycan core of the GPI moiety is the probable β-1,6-glucan attachment site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08607.x
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  • 2
    Electronic Resource
    Electronic Resource
    Sexual agglutination in Chlamydomonas eugametos is mediated by a single pair of hydroxyproline-rich glycoproteins (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 97 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The sexual mating reaction between gametes of the green alga Chlamydomonas eugametos starts by cell-cell contacts involving sex-specific cell-adhesion molecules (agglutinins) at the flagellar membrane. An in vitro adhesion assay is described using glutaraldehyde-fixed gametes. In vitro adhesion was fully comparable to in vivo adhesion, making it a reliable assay to study the initial recognition step of sexual adhesion in vivo. It was shown that both agglutinins are capable of inhibiting sexual adhesion at similar concentrations (1−2×10−10 M), indicating that mt+ and mt− agglutinins interact with each other during binding. This was confirmed by demonstrating that charcoal particles adsorbed with purified agglutinins of the opposite mating type aggregate with each other.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05447.x
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  • 3
    Electronic Resource
    Electronic Resource
    Transcription of multiple cell wall protein-encoding genes in Saccharomyces cerevisiae is differentially regulated during the cell cycle (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 161 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The yeast cell wall consists of an internal skeletal layer and an outside protein layer. The synthesis of both β-1,3-glucan and chitin, which together form the cell wall skeleton, is cell cycle-regulated. We show here that the expression of five cell wall protein-encoding genes (CWP1, CWP2, SED1, TIP1 and TIR1) is also cell cycle-regulated. TIP1 is expressed in G1 phase, CWP1, CWP2 and TIR1 are expressed in S/G2 phase, and SED1 in M phase. The data suggest that these proteins fulfil distinct functions in the cell wall.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb12967.x
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  • 4
    Electronic Resource
    Electronic Resource
    Dynamics of cell wall structure in Saccharomyces cerevisiae (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 26 (2002), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The cell wall of Saccharomyces cerevisiae is an elastic structure that provides osmotic and physical protection and determines the shape of the cell. The inner layer of the wall is largely responsible for the mechanical strength of the wall and also provides the attachment sites for the proteins that form the outer layer of the wall. Here we find among others the sexual agglutinins and the flocculins. The outer protein layer also limits the permeability of the cell wall, thus shielding the plasma membrane from attack by foreign enzymes and membrane-perturbing compounds. The main features of the molecular organization of the yeast cell wall are now known. Importantly, the molecular composition and organization of the cell wall may vary considerably. For example, the incorporation of many cell wall proteins is temporally and spatially controlled and depends strongly on environmental conditions. Similarly, the formation of specific cell wall protein–polysaccharide complexes is strongly affected by external conditions. This points to a tight regulation of cell wall construction. Indeed, all five mitogen-activated protein kinase pathways in bakers’ yeast affect the cell wall, and additional cell wall-related signaling routes have been identified. Finally, some potential targets for new antifungal compounds related to cell wall construction are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.2002.tb00613.x
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  • 5
    Electronic Resource
    Electronic Resource
    Green fluorescent protein-cell wall fusion proteins are covalently incorporated into the cell wall of Saccharomyces cerevisiae (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 162 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Tagging of two cell wall mannoproteins, Cwp1p and Cwp2p, in Saccharomyces cerevisiae with the green fluorescent protein from Aequorea victoria resulted in incorporation of fluorescent fusion proteins into the cell wall. Both living cells and isolated cell walls became brightly labeled. Intriguingly, the incorporation patterns of both fusion proteins differed. Western analysis of enzymatically released fusion proteins showed that they were covalently linked to the β-1,6-glucan part of the cell wall. Removal of the glycosylphosphatidyl-inositol anchor signal sequence of the green fluorescent protein-cell wall protein fusion proteins resulted in secretion of the proteins into the culture medium. These results indicate that green fluorescent protein-cell wall protein fusion proteins can be used as a convenient fluorescent marker to study the incorporation of specific cell wall proteins and the control mechanisms involved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13006.x
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  • 6
    Electronic Resource
    Electronic Resource
    The Aspergillus niger MADS-box transcription factor RlmA is required for cell wall reinforcement in response to cell wall stress (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 58 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In Aspergillus niger, the genes coding for glutamine:fructose-6-phosphate amidotransferase (gfaA) and α-1,3-glucan synthase (agsA) are induced in response to cell wall stress. In silico analysis of the promoter region of the two genes revealed the presence of putative DNA binding sites for transcription factors involved in stress responses, including sites identical to the Saccharomyces cerevisiae Rlm1p and Msn2p/Msn4p transcription factors. Promoter analysis indicated that the induction of the agsA gene in response to cell wall stress is fully dependent on a putative Rlm1p binding site in its promoter region. Database searches revealed the presence of S. cerevisiae Rlm1p homologues in most filamentous fungi examined, including A. niger. Deletion of the RLM1 homologue, named rlmA in A. niger, completely eliminated the induction of agsA and resulted in a twofold reduced induction of gfaA during Calcofluor White-induced cell wall stress. The rise in cell wall chitin in the presence of Calcofluor White was also affected in the rlmA deletion strain. In addition, the deletion strain was more sensitive towards cell wall stress agents. Our results indicate that A. niger responds to cell wall stress by transcriptional activation of cell wall reinforcing genes including agsA and gfaA through an Rlm1p-like transcription factor. We propose that such a cell wall salvage mechanism is wide spread in filamentous fungi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2005.04827.x
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  • 7
    Electronic Resource
    Electronic Resource
    Glucosylation of cell wall proteins in regenerating spheroplasts of Candida albicans (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 128 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The cell wall of Candida albicans contains mannoproteins that are covalently associated with β-1,6-glucan. When spheroplasts were allowed to regenerate a new cell wall, initially non-glucosylated cell wall proteins accumulated in the medium. While the spheroplasts became osmotically stable, β-1,6-glucosylated proteins could be identified in their cell wall by SDS-extraction or β-1,3-glucanase digestion. At later stages of regeneration, β-1,3-glucosylated proteins were also found. Hence, incorporation of proteins into the cell wall is accompanied by extracellular coupling to β-1,6-/β-l,3-glucan. The SDS-extractable glucosylated proteins probably represent degradation products of wall proteins rather than their precursors. Tunicamycin delayed, but did not prevent the formation of β-1,6-glucosylated proteins, demonstrating that β-1,6-glucan is not attached to N-glycosidic side-chains of wall proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07535.x
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  • 8
    Electronic Resource
    Electronic Resource
    Ultrastructure and properties of the sexual agglutinins of the biflagellate green alga Chlamydomonas moewusii (1989)
    Springer
    Sexual plant reproduction 2 (1989), S. 213-218 
    Details
    ISSN: 1432-2145
    Keywords: Cell adhesion ; Cell-cell recognition ; Chlamydomonas eugametos ; Chlamydomonas moewusii ; Sexual agglutinins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The mt− agglutinins of the interfertile species Chlamydomonas moewusii and Chlamydomonas eugametos are very similar fibrous molecules. The mt− agglutinin of C. moewusii has the same Stokes radius (39 nm) and sedimentation coefficient (9.3 S) as its counterpart in C. eugametos; its length (336 nm) and its ultrastructure, including the position of four kinks are also the same as in C. eugametos. The sugar compositions of both agglutinins are very similar, and they react equally well with the monoclonal antibody Mab 66.3 raised against the mt− agglutinin of C. eugametos. Finally, they are equally thermoresistant, with half-lives at 100 °C of 50 min (C. moewusii) and 57 min (C. eugametos). The mt+ agglutinins of both species are different. Both are fibrous molecules with a terminal head, but the fibrous part of the molecule in C. moewusii is shorter (210 nm compared to 276 nm). The mt+ agglutinin of C. moewusii is also significantly more sensitive to heating with a half-life of 6 min at 40 °C compared to the 20 min shown by the mt+ agglutinin of C. eugametos. Their sugar compositions are, however, very similar, and they react equally well with Mab 66.3. The mt+ agglutinin of C. moewusii is sensitive to denaturing reagents and proteolytic attack, whereas the mt− agglutinin is highly resistant. It is proposed that the globular head of the mt+ agglutinin acts as its recognition domain and interacts with a carbohydrate ligand on the mt− agglutinin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00195581
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  • 9
    Electronic Resource
    Electronic Resource
    Localization of arabinogalactan proteins in the membrane system of etiolated hypocotyls of Phaseolus vulgaris L. (1983)
    Springer
    Planta 159 (1983), S. 322-328 
    Details
    ISSN: 1432-2048
    Keywords: Arabinogalactan protein (localization) ; Hydroxyproline ; Phaseolus (arabinogalactan protein) ; Yariv reagent
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The subcellular distribution of arabinogalactan protein (AGP) in etiolated bean hypocotyls was studied by isopycnic density centrifugation on sucrose gradients at different Mg2+ concentrations. The distribution of hydroxyproline (a major amino acid in AGP) in the membrane-containing fractions indicated that hydroxyproline-containing proteins were associated with rough endoplasmic reticulum, possibly with the Golgi apparatus, and with the plasma membrane. Non-specific binding of hydroxyproline-containing molecules to membranes could be excluded. To detect AGPs, fractions obtained after isopycnic density centrifugation were isoelectrofocused on polyacrylamide gels, and the gels were stained with β-Gal-Yariv reagent. Bands appeared only at low pH values, where also most hydroxyproline was found. In the fractions at low densities (presumably membranefree), several bands were visible supporting the idea of the heterogeneous character of soluble AGP. The distribution of AGP in the membranous fractions strongly indicated that AGP was associated with the plasma membrane. Specific agglutination of protoplasts in the presence of β-Gal-Yariv reagent indicated that AGP was exposed at the outside of the cell membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00393170
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  • 10
    Electronic Resource
    Electronic Resource
    Composition and properties of the sexual agglutinins of the flagellated green alga Chlamydomonas eugametos (1987)
    Springer
    Planta 170 (1987), S. 314-321 
    Details
    ISSN: 1432-2048
    Keywords: Agglutinin ; Cell-cell recognition ; Chlamydomonas ; Hydroxyproline-rich glycoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sexual interaction between gametes of opposite mating type (mt) of the unicellular green alga Chlamydomonas eugametos starts with agglutination of the cells via particular glycoproteins on the flagellar surface. Purification of these socalled agglutinins was achieved by a three-step procedure consisting of, successively, gel filtration, anion-exchange chromatography, and high-performance gel filtration. The amino-acid and sugar compositions of both agglutinins showed a high degree of similarity; the most prominent amino acids were hydroxyproline, serine and glycine, and the main sugars were arabinose and galactose. The carbohydrate portions represented about half of the molecular mass of both agglutinins. Using high-performance gel filtration, a calibration curve was constructed for high-molecular-mass compounds from which the Stokes' radius of the sexual agglutinins could be estimated. The mt + agglutinin had a Stokes' radius of 39 nm and a sedimentation coefficient of 9.3 S. From these data its molecular mass was estimated to be 1.2·106. The corresponding data for the mt - agglutinin were 38 nm, 9.7 S and 1.3·106, respectively. The biological activity of both agglutinins was destroyed by mild periodate treatment. Treatment with specific glycosidases had a differential effect on the biological activity of the agglutinins. These observations indicate that carbohydrate side-chains are needed for biological activity and perhaps are responsible for the specifity of the sexual agglutinins. A comparison of both agglutinins is given and their possible structure is discussed in relation to their amino-acid and sugar compositions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00395022
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