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  • Nostoc commune  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 146 (1986), S. 87-95 
    ISSN: 1432-072X
    Keywords: Immobilized cells ; Gene expression ; Regulon ; nifH protein ; Desiccation ; Nostoc commune
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two-dimensional gel electrophoresis was used to analyze the effects of water stress (immobilization and rapid drying, desiccation, rewetting) on the protein index of the desiccation-tolerant cyanobacteriumNostoc commune UTEX 584. Five major “landmark” protein constellations were detected in the protein index of control cells (in liquid culture) and were designated A (1 protein), B (7 proteins), C (8 proteins), D (3 proteins) and E (2 proteins). These included proteins which showed different sensitivities to water stress. Upon immobilization and rapid drying of the cells at a water potential ({ie87-1}) of -99.5 MPa (aw=0.5) for 30 min, few changes took place in the index. Four conspicuous proteins and the majority of proteins in the size range 18 to 97 K diminished in abundance while most proteins of constellations A, B and C were detected in fluorographs with the same intensity as in the control. Although protein synthesis continued during this time of drying, no novel class of proteins was detected. The level of incorporation of35S in protein increased rapidly during the first 60 min of rehydration, and then decreased gradually for a further 2.5 h. Extant proteins that were hardly detectable after 24 h of drying, reappeared and increased in abundance upon rewetting of cells for 60 min while a number of proteins which disappeared after drying did not appear during this time. No novel class of proteins appeared upon rewetting. During further rehydration, extensive proteolysis was observed. ThenifH product (Fe protein of nitrogenase) was detected on Western blots — through cross-reaction with antibody — as an acidic polypeptide with a molecular mass of 33.8 K. Fe-protein was detected in immobilized cells after 30 min of drying, in desiccated material, and in rehydrated cells.
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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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