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  • 1
    Electronic Resource
    Electronic Resource
    Electron microscopy of photosynthetic membranes containing bacteriochlorophyll b (1983)
    Springer
    Archives of microbiology 135 (1983), S. 169-175 
    Details
    ISSN: 1432-072X
    Keywords: Photosynthetic membranes ; Electron microscopy ; Image processing ; Ectothiorhodospira halochloris ; Ectothiorhodospira abdelmalekii ; Rhodopseudomonas viridis ; Rhodopseudomonas sulfoviridis ; Thiocapsa pfennigii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414474
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  • 2
    Electronic Resource
    Electronic Resource
    Three-dimensional structure of a regular surface layer from Pseudomonas acidovorans (1986)
    Springer
    Archives of microbiology 144 (1986), S. 196-200 
    Details
    ISSN: 1432-072X
    Keywords: Pseudomonas acidovorans ; Cell-wall ; Surface layer ; 3-Dimensional reconstruction ; Image processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regular surface layer of Pseudomonas acidovorans was investigated by computer processing of a series of tilted view electron micrographs, and a reconstruction of the three-dimensional structure was obtained. The pattern is tetragonal and consists of massive identical subunits, block-like in face-view, which interlock loosely in a simple “cobblestone” pattern. The square unit cell has a lattice constant of 11 nm. The surface layer pattern of P. acidovorans appears to be more dependent on the underlying membrane for maintaining its integrity than those so far studied in other bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410946
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  • 3
    Electronic Resource
    Electronic Resource
    Functional analysis of the proteasome regulatory particle (1999)
    Springer
    Molecular biology reports 26 (1999), S. 21-28 
    Details
    ISSN: 1573-4978
    Keywords: ATPase ; proteasome ; S. cerevisiae ; ubiquitin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have developed S. cerevisiae as a model system for mechanistic studies of the 26S proteasome. The subunits of the yeast 19S complex, or regulatory particle (RP), have been defined, and are closely related to those of mammalian proteasomes. The multiubiquitin chain binding subunit (S5a/Mcb1/Rpn10) was found, surprisingly, to be nonessential for the degradation of a variety of ubiquitin-protein conjugates in vivo. Biochemical studies of proteasomes from Δrpn10 mutants revealed the existence of two structural subassemblies within the RP, the lid and the base. The lid and the base are both composed of 8 subunits. By electron microscopy, the base and the lid correspond to the proximal and distal masses of the RP, respectively. The base is sufficient to activate the 20S core particle for degradation of peptides, but the lid is required for ubiquitin-dependent degradation. The lid subunits share sequence motifs with components of the COP9/signalosome complex, suggesting that these functionally diverse particles have a common evolutionary ancestry. Analysis of equivalent point mutations in the six ATPases of the base indicate that they have well-differentiated functions. In particular, mutations in one ATPase gene, RPT2, result in an unexpected defect in peptide hydrolysis by the core particle. One interpretation of this result is that Rpt2 participates in gating of the channel through which substrates enter the core particle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006928316738
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  • 4
    Electronic Resource
    Electronic Resource
    Structural features of archaebacterial and eukaryotic proteasomes (1995)
    Springer
    Molecular biology reports 21 (1995), S. 11-20 
    Details
    ISSN: 1573-4978
    Keywords: electron microscopy ; multicatalytic protease ; proteasome ; Thermoplasma acidophilum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation. The molecule has a molecular mass of approximately 2000 kD and has a highly conserved structure in eukaryotes. The 26S proteasome is formed by a barrel-shaped 20S core complex and two polar 19S complexes. The 20S complex has C2 symmetry and is formed by four seven-membered rings of which the outer rings (α-type subunits) are rotated by 25.7° relative to the inner rings while the inner rings (β-type subunits) are in register. From a comparison of the activity and regulation of the 26S and 20S particles it can be deduced that the 20S particle contains the protease activity while the 19S complex contains isopeptidase, ATPase and protein unfolding activities. In this article we describe the structures of various proteasome complexes as determined by electron microscopy and discuss structural implications of their subunit sequences.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00990965
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  • 5
    Electronic Resource
    Electronic Resource
    Eubacterial proteasomes (1997)
    Springer
    Molecular biology reports 24 (1997), S. 125-131 
    Details
    ISSN: 1573-4978
    Keywords: proteasome ; HslVU ; Clp ; multicatalytic protease ; ATP-dependent proteolysis ; Rhodococcus erythropolis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependent pathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease of about 700 kDa, which has also been detected in archaebacteria and, more recently, in eubacteria. Currently, the distribution of 20S proteasomes in eubacteria appears limited to the actinomycetes, while most other eubacteria contain a related complex of simpler structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006803512761
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  • 6
    Electronic Resource
    Electronic Resource
    Structural features of archaebacterial cell envelopes (1992)
    Springer
    Journal of bioenergetics and biomembranes 24 (1992), S. 567-575 
    Details
    ISSN: 1573-6881
    Keywords: S layers ; surface glycoproteins ; plasma membrane ; electron crystallography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Regularly arrayed surface (glyco)proteins—often referred to as S layers—are a common feature of the cell envelopes of almost all archaebacteria. We have selected some examples (Halobacterium, Sulfolobus, Thermoproteus, Pyrobaculum, Staphylothermus), and we describe the structure of their surface layers as revealed primarily by electron crystallography. In spite of a considerable diversity in shapes and dimensions, some common structural features emerge from the comparison. The glycoprotein arrays are composed of oligomeric units which are anchored in the plasma membrane; extended spacer or linker domains maintain the bulk of the more or less porous surface layers at a constant distance above the membrane surface, thus creating a quasi-periplasmic compartment. Functions ascribed to surface layers, such as compartmentalization, shape maintenance and determination, and adhesion are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762349
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  • 7
    Electronic Resource
    Electronic Resource
    A self-compartmentalizing protease in Rhodococcus: the 20S proteasome (1998)
    Springer
    Antonie van Leeuwenhoek 74 (1998), S. 83-87 
    Details
    ISSN: 1572-9699
    Keywords: Rhodococcus ; Mycobacterium ; proteasome ; multi-subunit protease ; AAA-family ATPase ; actinomycetes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1001708012708
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  • 8
    Electronic Resource
    Electronic Resource
    Surface structure variants inDeinococcus radiodurans (1987)
    Springer
    Current microbiology 16 (1987), S. 15-20 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The cell wall morphology and the polypeptide composition of two different strains as well as of two spontaneous mutants ofDeinococcus radiodurans have been compared. The two strains differ with respect to the density of their carbohydrate coat. One of the mutants lacks the surface (HPI) layer; the other one is devoid of a carbohydrate coat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01568163
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  • 9
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    Three-dimensional structure of a regular surface layer from Pseudomonas acidovorans (1986)
    Springer
    Details
    Publication Date: 1986-04-01
    Print ISSN: 0302-8933
    Electronic ISSN: 1432-072X
    Topics: Biology
    Published by Springer
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  • 10
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    Electron microscopy of photosynthetic membranes containing bacteriochlorophyll b (1983)
    Springer
    Details
    Publication Date: 1983-09-01
    Print ISSN: 0302-8933
    Electronic ISSN: 1432-072X
    Topics: Biology
    Published by Springer
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