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  • 1
    Digitale Medien
    Digitale Medien
    An outer membrane protein (OmpA) of Escherichia coli can be translocated across the cytoplasmic membrane of Bacillus subtllis (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 9 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: The translocation of secretory proteins derived from a Gram-positive (Staphylococcus hyicus prolipase) or a Gram-negative (Escherichia coli pre-OmpA protein) bacterium across the cytoplasmic membrane was studied in E. coli and Bacillus subtilis. in both microorganisms, the prolipase was found to be secreted across the plasma membrane when either the pre-prolipase signal peptide (38 amino acids in length) or the pre-OmpA signal peptide (21 amino acids in length) was used. Expression of the gene encoding the authentic pre-OmpA protein in B. subtilis resulted in the translocation of mature OmpA protein across the plasma membrane. Processing of the OmpA precursor in B. subtilis required the electrochemical potential and was sensitive to sodium azide, suggesting that the B. subtilis SecA homologue was involved in the translocation process. The mature OmpA protein, which was most likely present in an aggregated state, was fully accessible to proteases in protoplasted cells. Therefore, our results clearly demonstrate that an outer membrane protein can be secreted by B. subtilis, supporting the notion that the basic mechanism of protein translocation is highly conserved in Gram-positive and Gram-negative bacteria.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01743.x
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  • 2
    Digitale Medien
    Digitale Medien
    Isolation and characterization of a Bacillus subtilis secA mutant allele conferring resistance to sodium azide (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 124 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract A mutation has been isolated in the Bacillus subtilis secA gene (secA10) which allows cell growth and residual protein translocation in the presence of 1.5 mM sodium azide. Besides conferring resistance to sodium azide, the corresponding SecA10 mutant protein, in which glutamic acid at position 338 has been changed to glycine, seems to possess a secretion defect even in the absence of azide. In addition, the secA10 mutant protein was found to be recessive to wild-type secA with regard to azide resistance. Our results strongly suggest that, like the situation in Escherichia coli, the B. subtilis SecA protein is a main target for the lethal action of sodium azide.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07314.x
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  • 3
    Digitale Medien
    Digitale Medien
    The Staphylococcus carnosus secE gene: Cloning, nucleotide sequence, and functional characterization in Escherichia coli secE mutant strains (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 117 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract A DNA fragment containing the genes secE, nusG and rplK of Staphylococcus carnosus was cloned using the Escherichia coli rplK gene as a probe. The S. carnosus secE homologue encodes a protein of 65 amino acid residues which is homologous to the carboxyl-terminal region of the E. coli SecE protein. The S. carnosus SecE polypeptide which, in contrast to the E. coli SecE protein, contains only one putative transmembrane segment, could fully replace the E. coli SecE protein in two different secE mutants. These results strongly suggest that the identified secE gene encodes an important component of the S. carnosus protein export apparatus.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06751.x
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  • 4
    Digitale Medien
    Digitale Medien
    Export and sorting of theEscherichia coli outer membrane protein OmpA (1990)
    Springer
    Journal of bioenergetics and biomembranes 22 (1990), S. 441-449 
    Details
    ISSN: 1573-6881
    Schlagwort(e): Escherichia coli ; plasma membrane ; outer membrane ; OmpA ; protein translocation/sorting
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Physik
    Notizen: Abstract Results of studies, mostly using the outer membrane, 325 residue protein OmpA, are reviewed which concern its translocation across the plasma membrane and incorporation into the outer membrane ofEscherichia coli. For translocation, neither a unique export signal, acting in a positive fashion within the mature part of the precursor, nor a unique conformation of the precursor is required. Rather, the mature part of a secretory protein has to be export-compatible. Export-incompatibility can be caused by a stretch of 16 (but not 8 or 12) hydrophobic residues, too low a size of the polypeptide (smaller than 75 residue precursors), net positive charge at the N-terminus, or lack of a turn potential at the same site. It is not yet clear whether binding sites for chaperonins (SecB, trigger factor, GroEL) within OmpA are importantin vivo. The mechanism of sorting of outer membrane proteins is not yet understood. The membrane part of OmpA, encompassing residues 1 to about 170, it thought to traverse the membrane eight times in antiparallel β-sheet conformation. At least the structure of the last β-strand (residues 160–170) is of crucial importance for membrane assembly. It must be amphiphilic or hydrophobic, these properties must extend over at least nine residues, and it must not contain a proline residue at or near its center. Membrane incorporation of OmpA involves a conformational change of the protein and it could be that the last β-strand initiates folding and assembly in the outer membrane.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00763176
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  • 5
    Digitale Medien
    Digitale Medien
    Abscheidung von Quecksilber aus Abgasen im Festbett aus Aktivkohle und Inertmaterial (1999)
    Weinheim : Wiley-Blackwell
    Chemie Ingenieur Technik - CIT 71 (1999), S. 1191-1194 
    Details
    ISSN: 0009-286X
    Schlagwort(e): Chemistry ; Industrial Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Zusätzliches Material: 8 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/cite.330711018
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