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  • 1
    Electronic Resource
    Electronic Resource
    Translation elongation factor-3 (EF-3): An evolving eukaryotic ribosomal protein? (1995)
    Springer
    Journal of molecular evolution 41 (1995), S. 376-387 
    Details
    ISSN: 1432-1432
    Keywords: Elongation factor 3 ; EF-3 ; Translation ; Ribosomal protein ; Fungal protein synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Fungi appear to be unique in their requirement for a third soluble translation elongation factor. This factor, designated elongation factor 3 (EF-3), exhibits ribosome-dependent ATPase and GTPase activities that are not intrinsic to the fungal ribosome but are nevertheless essential for translation elongation in vivo. The EF-3 polypeptide has been identified in a wide range of fungal species and the gene encoding EF-3 (YEF3) has been isolated from four fungal species (Saccharomyces cerevisiae, Candida albicans, Candida guillermondii, andPneumocystis carinii). Computer-assisted analysis of the predictedS. cerevisiae EF-3 amino acid sequence was used to identify several potential functional domains; two ATP binding/catalytic domains conserved with equivalent domains in members of the ATP-Binding Cassette (ABC) family of proteins, an aminoterminal region showing significant similarity to theE. coli S5 ribosomal protein, and regions of predicted interaction with rRNA, tRNA, and mRNA. Furthermore, EF-3 was also found to display amino acid similarity to myosin proteins whose cellular function is to provide the motive force of muscle. The identification of these regions provides clues to both the evolution and function of EF-3. The predicted functional regions are conserved among all known fungal EF-3 proteins and a recently described homologue encoded by the Chlorella virus CVK2. We propose that EF-3 may play a role in the ribosomal optimization of the accuracy of fungal protein synthesis by altering the conformation and activity of a ribosomal “accuracy center,” which is equivalent to the S4-S5-S12 ribosomal protein accuracy center domain of theE. coli ribosome. Furthermore, we suggest that EF-3 represents an evolving ribosomal protein with properties analogous to the intrinsic ATPase activities of higher eukaryotic ribosomes, which has wider implications for the evolutionary divergence of fungi from other eukaryotes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01215185
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Translation elongation factor-3 (EF-3): An evolving eukaryotic ribosomal protein? (1995)
    Springer
    Journal of molecular evolution 41 (1995), S. 376-387 
    Details
    ISSN: 1432-1432
    Keywords: Elongation factor 3 ; EF-3 ; Translation ; Ribosomal protein ; Fungal protein synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Fungi appear to be unique in their requirement for a third soluble translation elongation factor. This factor, designated elongation factor 3 (EF-3), exhibits ribosome-dependent ATPase and GTPase activities that are not intrinsic to the fungal ribosome but are nevertheless essential for translation elongation in vivo. The EF-3 polypeptide has been identified in a wide range of fungal species and the gene encoding EF-3 (YEF3) has been isolated from four fungal species (Saccharomyces cerevisiae, Candida albicans, Candida guillermondii, and Pneumocystis carinii). Computer-assisted analysis of the predicted S. cerevisiae EF-3 amino acid sequence was used to identify several potential functional domains; two ATP binding/catalytic domains conserved with equivalent domains in members of the ATP-Binding Cassette (ABC) family of proteins, an aminoterminal region showing significant similarity to the E. coli S5 ribosomal protein, and regions of predicted interaction with rRNA, tRNA, and mRNA. Furthermore, EF-3 was also found to display amino acid similarity to myosin proteins whose cellular function is to provide the motive force of muscle. The identification of these regions provides clues to both the evolution and function of EF-3. The predicted functional regions are conserved among all known fungal EF-3 proteins and a recently described homologue encoded by the Chlorella virus CVK2. We propose that EF-3 may play a role in the ribosomal optimization of the accuracy of fungal protein synthesis by altering the conformation and activity of a ribosomal “accuracy center,” which is equivalent to the S4-S5-S12 ribosomal protein accuracy center domain of the E. coli ribosome. Furthermore, we suggest that EF-3 represents an evolving ribosomal protein with properties analogous to the intrinsic ATPase activities of higher eukaryotic ribosomes, which has wider implications for the evolutionary divergence of fungi from other eukaryotes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00186550
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Intracellular concentration of elements in normal and dystrophic skeletal muscles of the chicken (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 103 (1980), S. 193-200 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In this study, the intracellular concentrations of six elements (mmole/kg dry weight) were directly measured in the muscle fibers of pectoralis major muscles of eight week old, genetically dystrophic and normal chickens by the X-ray microanalysis technique. The extent of muscle degeneration was evaluated by morphometric measurements of muscle fiber diameter and other histological changes. A significant increase in the concentration of intracellular sodium and chlorine was evident in dystrophic muscles. The concentration of intracellular sodium was 127.0 ± 35.0 in the muscle fibers of dystrophic chicks compared to 65.7 ± 16.5 in normal controls. The concentration of chlorine was 90.5 ± 27.5 and 54.1 ± 5.5 in the muscle fibers of dystrophic and normal chicks respectively. The intracellular concentrations of potassium, magnesium, phosphorous, and sulfur remained unchanged in the dystrophic condition. Morphometric studies revealed that the dystrophic pectoralis muscles contain fewer but thicker fibers per unit area compared to normal pectoralis muscles. The importance of these findings are discussed in relation to the results of earlier investigations.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041030204
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Elemental content in the nucleus and in yolk and yolk-free cytoplasm of developing Rana pipiens oocytes: An X-ray microanalysis study (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 109 (1981), S. 91-97 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Energy dispersive x-ray microanalysis measured the Na, K, Cl, P, Mg, S, and Ca contents (mM/kg dry weight) in the nucleus, yolk-free cytoplasm, and yolk platelets of Rana pipiens oocytes quick frozen in the ovary. The data revealed that significant content changes occur in frog oocytes during intraovarian growth. All elements but Ca changed in content in the nucleus and cytoplasm, while in the yolk platelet only Na content did not change. A nucleus to cytoplasm K gradient develops and increases in magnitude during oocyte growth. The data from this and previous reports lead to the hypothesis that intra-oocytic water and elements undergo changes in state during oocyte growth and that three subcellular Na compartments exist.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041090111
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Role of plasma membrane and of cytomatrix in maintenance of intracellular to extracellular ion gradients in chicken erythrocytes (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 137 (1988), S. 299-304 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Ultrastructural observations in combination with electron probe X-ray microanalysis on detergent (Brij 58) permeabilized (disruption of the plasma membrane) nucleated chicken erythrocytes support the view that a large fraction of cytoplasmic and nuclear K+ is not freely diffusible and that adsorption of K+ on detergent released mobilizable proteins exists within the cell. The data also suggest that the detergent proteins are normally immobilized by a detergent-resistant cytoskeleton so that they are not immediately free to diffuse from the cell for several minutes after detergent disruption of the plasma membrane.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041370213
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    Paper (German National Licenses)
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