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  • AAA-family ATPase  (1)
  • Electron microscopy  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Archives of microbiology 135 (1983), S. 169-175 
    ISSN: 1432-072X
    Schlagwort(e): Photosynthetic membranes ; Electron microscopy ; Image processing ; Ectothiorhodospira halochloris ; Ectothiorhodospira abdelmalekii ; Rhodopseudomonas viridis ; Rhodopseudomonas sulfoviridis ; Thiocapsa pfennigii
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The photosynthetic membranes of the five bchl b-containing bacteria Ectothiorhodospira halochloris, E. abdelmalekii, Rhodopseudomonas viridis, R. sulfoviridis and Thiocapsa pfennigii have been investigated by electron microscopy and digital image analysis. All five species have the photosynthetic complexes hexagonally arrayed in the membrane with lattice spacings close to 13 nm, except for R. sulfoviridis and T. pfennigii which display somewhat smaller (∼12.5 nm) lattice spacings. Correlation averaging which imposes less stringent requirements on the lattice perfection than conventional Fourier filtration techniques has been employed to elucidate the structure of the photosynthetic complexes. Their basic organization, i.e. a ring, probably containing the light-harvesting (LH) polypeptides, surrounding a core (the “reaction centre”) appears to be almost identical for all species under scrutiny. Despite a resolution of ∼1.6 nm, however, little further significant substructure can be deduced from the averages; possible reasons for the “blurred” appearance of the LH-ring and absence of any subdivision in the reaction centre are discussed along with strategies aimed at obtaining a more detailed model of the molecular architecture of the photosynthetic membranes.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Antonie van Leeuwenhoek 74 (1998), S. 83-87 
    ISSN: 1572-9699
    Schlagwort(e): Rhodococcus ; Mycobacterium ; proteasome ; multi-subunit protease ; AAA-family ATPase ; actinomycetes
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The 26S proteasome represents a major, energy-dependent and self- compartmentalizing protease system in eukaryotes. The proteolytic core of this complex, the 20S proteasome, is also ubiquitous in archaea. Although absent from most eubacteria, this multi- subunit protease was recently discovered in Rhodococcus and appears to be confined to actinomycetes. The eubacterial 20S proteasome represents an attractive complementary system to study proteasome assembly, quaternary structure, and catalytic mechanism. In addition, it is likely to contribute substantially to our understanding of the role of various self-compartmentalizing proteases in bacterial cells.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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