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  • 1
    ISSN: 1615-6102
    Keywords: UV-absorbing pigments ; Protein secretion ; Capsule ; Glycoproteins ; Trehalose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Filaments of the desiccation-tolerant cyanobacteriumNostoc commune are embedded within, and distributed throughout, a dense glycan sheath. Analysis of the glycan of field materials and of pure cultures ofN. commune DRH 1 through light and electron microscopy, immunogold labelling and staining with dyes, revealed changes in the pattern of differentiation in glycan micro-structure, as well as localized shifts in pH, upon rehydration of desiccated field material. A Ca/Si rich external (pellicular) layer of the glycan acts as a physical barrier to epiphytic bacteria on the surface ofN. commune colonies. A purified fraction (〉12 kDa) of an aqueous extract of the glycan from desiccated field material contained glucose, N-acetylglucosamine, glucosamine, mannose, and galactosamine with ratios of 3.1∶1.4∶1∶0.1∶0.06, respectively. Lipid soluble extracts ofN. commune contained trehalose and sucrose and the levels of both became undetectable following cell rehydration. Intracellular cyanobacterial trehalase was identified using immunoblotting and its synthesis was detected upon rehydration of desiccated field cultures. Elemental analysis of glycan extracts showed a flux in the concentrations of salts in the glycan matrix following rehydration of desiccated colonies. Water-stress proteins (Wsp; most abundant proteins in glycan), a water soluble UV-A/B-absorbing pigment, the lipid-soluble UV-protective pigment scytonemin (in both its oxidized and reduced forms), as well as two unidentified cyanobacterial glycoproteins (75 kDa and 110 kDa), were found within the glycan matrix. An unidentified 68 kDa protein, the second most abundant protein in aqueous extracts of the glycan, was isolated and its N-terminal sequence was determined as AFIFGTISPNNLSGTSGNSGIVGSA. Gene bank searches with this sequence identified significant homologies (35–45%) with various carbohydrate-modifying enzymes. The role of the glycan in the desiccation tolerance ofN. commune is discussed with respect to structure/function relationships.
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  • 2
    ISSN: 1573-5176
    Keywords: Cyanobacteria ; Nostoc commune ; glycan ; phase transition ; membrane ; desiccation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cells of the cyanobacterium Nostoc commune secrete a complex, high molecular weight, extracellular polysaccharide (EPS) which accumulates to more than 60% of the dry weight of colonies. The EPS was purified from the clonal isolate N. commune DRH1. The midpoint of the membrane phase transition (Tm) of desiccated cells of N. commune CHEN was low (Tm dry = 8 °C) and was comparable to the Tm of rehydrated cells((Tm)H20 = 6 °C). The EPS was not responsible for the depression of Tm. However, the EPS, at low concentrations, inhibited specifically the fusion of phosphatidylcholine membrane vesicles when they were dried in vitro at0% relative humidity (−400 MPa). Low concentrations of a trehalose:sucrose mixture, in a molar ratio which corresponded with that present in cells in vivo, together with small amounts of the EPS, were efficient in preventing leakage of carboxyfloroscein (CF) from membrane vesicles. Freeze-fracture electron microscopy resolved complex changes in the structure of the EPS and the outer membrane in response to rehydration of desiccated cells. The capacity of the EPS to prevent membrane fusion, the maintenance of a low Tm dry in desiccated cells, and the changes in rheological properties of the EPS in response to water availability, constitute what are likely important mechanisms for desiccation tolerance in this cyanobacterium.
    Type of Medium: Electronic Resource
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