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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 42 (1970), S. 941-942 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 14 (1980), S. 527-537 
    ISSN: 0091-7419
    Keywords: leucine transport genes ; cloning ; regulation ; rho factor ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Leucine is transported into E coli by two osmotic shock-sensitive, high-affinity systems (LIV-I and leucine-specific systems) and one membrane bound, low-affinity system (LIV-II). Expression of the high-affinity transport systems is altered by mutations in liv R and 1st R, genes for negatively acting regulatory elements, and by mutations in rho, the gene for transcription termination. All four genes for high-affinity leucine transport (livJ, livK, livH, and livG) are closely linked and have been cloned on a plasmid vector, pOX1. Several subcloned fragments of this plasmid have been prepared and used in complementation and regulation studies. The results of these studies suggest that livJ and livK are separated by approximately one kilobase and give a gene order of livJ-livK-livH. livJ and livK appear to be regulated in an interdependent fashion; livK is expressed maximally when the livJ gene is inactivated by mutation or deletion. The results support the existence of separate promoters for the livJ and livK genes. The effects of mutations in the rho and livR genes are additive on one another and therefore appear to be involved in independent regulatory mechanisms. Mutations in the rho gene affect both the LIV-I and leucinespecific transport systems by increasing the expression of livJ and livK, genes for the LIV-specific and leucine-specific binding proteins, respectively.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 6 (1977), S. 419-431 
    ISSN: 0091-7419
    Keywords: regulation ; amino acid transport ; mutants ; leucine sensitivity ; leucine ; isoleucine ; valine ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Leucine is transported into E. coli cells by high-affinity transport systems (LIV-I and leucine-specific systems) which are sensitive to osmotic shock and require periplasmic binding proteins. In addition leucine is transported by a low-affinity system (LIV-II) which is membrane bound and retained in membrane vesicle preparations. The LIV-I system serves for threonine and alanine in addition to the 3 branched-chain amino acids. The LIV-II system is more specific for leucine, isoleucine, and valine while the high-affinity leucine-specific system has the greatest specificity.A regulatory locus, livR at minute 22 on the E. coli chromosome produces negatively regulated leucine transport and synthesis of the binding proteins. Valine-resistant strains have been selected to screen for transport mutants. High-affinity leucine transport mutants that have been identified include a LIV-binding protein mutant, livJ, a leucine-specific binding protein mutant livK and a nonbinding protein component of the LIV-I system, livH. A fourth mutant, livP, appears to be required only for the low-affinity LIV-II system. The existence of this latter mutant indicates that LIV-I and LIV-II are parallel transport systems. The 4 mutations concerned with high-affinity leucine transport form a closely linked cluster of genes on the E. coli chromosome at minute 74.The results of recent studies on the regulation of the high-affinity transport systems suggests that an attenuator site may be operative in its regulation. This complex regulation appears to require a modified leucyl-tRNA along with the transcription termination factor rho. Regulation of leucine transport is also defective in relaxed strains.Among the branched-chain amino acids only leucine produces regulatory changes in LIV-I activity suggesting a special role of this amino acid in the physiology of E. coli. It was shown that the rapid exchange of external leucine for intracellular isoleucine via the LIV-I system could create an isolucine pseudoauxotrophy and account for the leucine sensitivity of E. coli.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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