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  • 1
    Electronic Resource
    Electronic Resource
    Topological and functional studies on HlyB of Escherichia coli (1992)
    Springer
    Molecular genetics and genomics 232 (1992), S. 40-48 
    Details
    ISSN: 1617-4623
    Keywords: E. coli haemolysin ; Secretion of haemolysin ; Topology and function of HlyB
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The topology of HlyB, a protein located in the inner membrane of Escherichia coli and involved in the secretion of α-haemolysin (HlyA), was determined by the generation of HlyB-PhoA and HlyB-LacZ fusion proteins. The data obtained by this biochemical method together with computer predictions suggest that HlyB is inserted in the cytoplasmic membrane by six stable hydrophobic, α-helical transmembrane segments. These segments extend from amino acid positions 158 to 432 of HlyB. The cytoplasmic loops between these transmembrane segments are relatively large and carry an excess of positively charged amino acids, while the periplasmic loops are rather small. In addition to these six transmembrane segments, two additional regions in the 78 N-terminal amino acids of HlyB appear to be also inserted in the cytoplasmic membrane. However, the association of these two segments with the cytoplasmic membrane seems to be less tight, since active PhoA and LacZ fusions were obtained by insertion into the same positions of these segments. A LacZ-HlyAs fusion protein carrying, at the C-terminus of LacZ, the 60-amino acid signal sequence of HlyA was not secreted in the presence of HlyB/HlyD. However, transport of this fusion protein into the cytoplasmic membrane appeared to be initiated, as suggested by the tight association of this protein with the inner membrane. A similar close association of LacZ-HlyAs with the inner membrane was also observed in the presence of HlyB alone but not in its absence. These data suggest that HlyB recognizes the HlyA signal sequence and initiates the transport of HlyA into the membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00299135
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  • 2
    Electronic Resource
    Electronic Resource
    A topological model for the haemolysin translocator protein HlyD (1992)
    Springer
    Molecular genetics and genomics 234 (1992), S. 155-163 
    Details
    ISSN: 1617-4623
    Keywords: Escherichia coli haemolysin ; Secretion of haemolysin ; Topology and function of HlyD
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A topological model for HlyD is proposed that is based on results obtained with gene fusions of lacZ and phoA to hlyD. Active H1yD-LacZ fusion proteins were only generated when lacZ was fused to hlyD. within the first 180 by (60 amino acids). H1yD-PhoA proteins exhibiting alkaline phosphatase (AP) activity were obtained when phoA was inserted into hlyD. between nucleotides 262 (behind amino acid position 87) and 1405 (behind amino acid position 468, only 10 amino acids away from the C-terminus of HlyD Active insertions of phoA into the middle region of hlyD. were not observed on in vivo transposition but such fusions exhibiting AP activity could be constructed by in vitro techniques. A fusion protein that carried the PhoA part close to the C-terminal end of HlyD proved to be the most stable HlyD-PhoA fusion protein. In contrast to the other, rather unstable, HlyD-PhoA+ fusions, no proteolytic degradation product of this HlyD-PhoA protein was observed and nearly all the alkaline phosphatase activity was membrane bound. Protease accessibility and cell fractionation experiments indicated that the alkaline phosphatase moiety of this fusion protein was located in the periplasm as for all other HlyD-PhoA+ proteins. These data and computer-assisted predictions suggest a topological model for HlyD with the N-terminal 60 amino acids located in the cytoplasm, a single transmembrane segment from amino acids 60 to 80 and a large periplasmic region extending from amino acid 80 to the C-terminus. Neither the HlyD fusion proteins obtained nor a mutant HlyD protein that had lost the last 10 amino acids from the C-terminus of HlyD exhibited translocator activity for HlyA or other reporter proteins carrying the HlyA signal sequence. The C-terminal 10 amino acids of HlyD showed significant similarity with the corresponding sequences of other HlyD-related proteins involved in protein secretion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00272357
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  • 3
    Electronic Resource
    Electronic Resource
    Extrachromosomale DNA in Bakterien (1973)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 85 (1973), S. 569-580 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In vielen Bakterienzellen treten zusätzlich zur chromosomalen DNA, welche die genetische Information der Zelle enthält, kleinere ringförmige DNA-Faktoren auf, die als Plasmide oder Episomen bezeichnet werden. Diese genetischen Elemente verleihen der Zelle zusätzliche biochemische Fähigkeiten. Beschrieben werden die Fertilitätsfaktoren (F und F′), die Antibiotika-Resistenz-Faktoren (R), die Colicinogenen Faktoren (Col), die Hämolytischen Faktoren (Hly) und andere extrachromosomale DNA-Systeme. Diese kleinen DNA-Moleküle lassen sich isolieren und eignen sich somit besonders, um Fragen der DNA-Replikation und der stabilen Etablierung von genetischem Material in der Bakterienzelle zu untersuchen.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19730851303
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  • 4
    Electronic Resource
    Electronic Resource
    Extrachromosomal DNA in Bacteria (1973)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 12 (1973), S. 517-528 
    Details
    ISSN: 0570-0833
    Keywords: Extrachromosomal DNA ; Bacteria ; DNA ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In addition to chromosomal DNA carrying the genetic information of the cell, many bacterial cells contain smaller circular DNA factors known as plasmids or episomes. These genetic elements endow the cell with additional biochemical capabilities. The fertility factors (F and F′), the antibiotic resistance factors (R), the colicinogenic factors (Col), the hemolytic factors (Hly), and other extrachromosomal DNA systems are described. These small DNA molecules can be isolated, and are therefore particularly suitable for the investigation of DNA replication and the stable establishment of genetic material in the bacterial cell.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.197305171
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