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  • 1
    Electronic Resource
    Electronic Resource
    RNA-directed cell-free synthesis of the galactose enzymes of Escherichia coli (1973)
    Springer
    Molecular genetics and genomics 124 (1973), S. 329-344 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Conditions are described for the RNA-directed cell-free synthesis of the three galactose enzymes of Escherichia coli. Together with the DNA-directed synthesis described previously, this system permits the measurement of the three gene-products encoded by the gal operon as active enzymes synthesized in vitro in response to either gal-DNA or gal-RNA. The yield of enzyme is proportional to the amount of RNA added. Thus, the RNA-directed enzyme synthesis can serve as an assay system for functional mRNA. This test has been employed to determine the kinetics of synthesis and degradation of functional gal mRNA under the conditions of cell-free enzyme synthesis. The functional half-life of gal mRNA in this system is 6–7 minutes and is higher than expected from in vivo measurements. In contrast to the DNA-directed cell-free synthesis, the RNA-directed synthesis of the galactose enzymes is neither stimulated by cyclic adenosine-3′:5′-monophosphate nor by inducer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267662
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of different conformations of galactose messenger RNA on gene expression and messenger half-life in vitro (1975)
    Springer
    Molecular genetics and genomics 136 (1975), S. 41-54 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary From a DNA-directed cell-free system, functional gal mRNA is obtained which directs the cell-free synthesis of the three galactose enzymes of Escherichia coli. A substantial fraction of this gal mRNA has the properties of a polycistronic messenger. Exposure to elevated temperatures in the presence or absence of magnesium ion results in pronounced changes of the capacity of this mRNA to give rise to the synthesis of the three enzymes. Depending on the conditions of the pre-treatment, the absolute amounts as well as the ratio of the three gene products synthesized can be changed. The different forms of gal messenger so obtained also exhibit different susceptibilities towards functional inactivation during the enzyme synthesis reaction. As the changes in template activity are reversible, it is concluded that the different treatments cause reversible transitions between different conformations of the gal mRNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00275447
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  • 3
    Electronic Resource
    Electronic Resource
    Control of formation of active soluble or inactive insoluble baker's yeast α-glucosidase PI in Escherichia coli by induction and growth conditions (1989)
    Springer
    Molecular genetics and genomics 216 (1989), S. 149-155 
    Details
    ISSN: 1617-4623
    Keywords: α-Glucosidase ; Active expression ; Escherichia coli ; Refractile bodies ; Protein folding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Using standard growth conditions (LB medium, 37°C, induction with 5 mM IPTG) yeast α-glucosidase PI expressed under the control of the regulated tac-hybrid promoter results in the synthesis of insoluble aggregated α-glucosidase granules in Escherichia coli. Under these conditions active soluble α-glucosidase amounts to less than 1% of the heterologously produced protein. However, the amount of soluble active α-glucosidase was dramatically increased when the strong tac-hybrid promoter was to a limited extent induced. This was achieved at concentrations of 0.01 mM IPTG or of 1% lactose or lower in a lactosepermease deficient host strain containing the lacI qrepressor gene on an R-plasmid. The formation of active soluble α-glucosidase was almost 100% when E. coli cells induced in this manner were cultivated under conditions that reduced growth rate, i.e. at decreased temperature, extreme pH values or in minimal and complete media supplemented with different carbon sources.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00332244
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  • 4
    Electronic Resource
    Electronic Resource
    Processing by OmpT of fusion proteins carrying the HlyA transport signal during secretion by theEscherichia coli hemolysin transport system (1992)
    Springer
    Molecular genetics and genomics 233 (1992), S. 42-48 
    Details
    ISSN: 1617-4623
    Keywords: Secretion ; Recombinant DNA ; Hemolysin ; HlyB/H1yD complementation ; OmpT protease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A fusion gene (ces-hlyA s) was constructed by ligating the genetic information for the C-terminal 60 amino acids (hlyA s) ofEscherichia coli hemolysin (H1yA) to the ces gene for a cholesterol esterase/lipase (CE) from aPseudomonas species. Part (about 30 %) of the expressed fusion protein CE-H1yAs was secreted inE. coli carryinghlyB andhlyD genes. Following the insertion between the reporter gene andhlyA s of a linker sequence that contains the information for potential cleavage sites for the outer membrane protease OmpT, two different fusion proteins (PhoA-H1yAs and CE-HlyAs) were shown to be cleaved by OmpT between the two parts during H1yB/H1yD-mediated secretion. Processed PhoA and CE accumulated in the supernatant. The efficiency of cleavage by OmpT was considerably improved by increasedompT gene dose. It was further shown that OmpT preferentially recognizes potential cleavage sites within the linker sequence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00587559
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  • 5
    Electronic Resource
    Electronic Resource
    Cloning and characterization of Baker's yeast α-glucosidase: Over-expression in a yeast strain devoid of vacuolar proteinases (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 5 (1989), S. 11-24 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; α-glucosidase ; nucleotide sequence ; expression ; proteinase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two α-glucosidase (maltase) genes, designated GLUCPI and GLUCPII, have been cloned from an industrial strain of baker's yeast (Saccharomyces cerevisiae) by complementation of a maltase-negative mutant strain. The different genes were identified according to their alternatively expressed isoenzymes PI and PII in transformants after isoelectric focusing and activity staining in separated cell lysates. The gene encoding α-glucosidase PI (GLUCPI), which was not present in laboratory strains of S. carlsbergensis with a defined MAL1, 2, 3, 4 or 6 locus, was sequenced and compared with the recently published MAL6S gene. This comparison revealed single amino acid deviations at three positions in the predicted polypeptide sequence. In addition, the divergent promoter region of GLUCPI differed from MAL6S by a triple repeated 147-bp DNA segment. Maltose induction and glucose repression of α-glucosidase PI were not affected by the deletion of the repeated DNA segment. However, the absolute expression of α-glucosidase PI increased two- to four-fold. In addition, a two-fold increase in the maltase synthesis occurred when the cloned positive regulator gene MAL2-8cp was on the same plasmid. Furthermore, stability of the α-glucosidase in cultures in the stationary growth phase was greatly enhanced using a host strain lacking the proteinases A and B and the carboxypeptidases Y and S. Promoter trimming, MAL2-8cp stimulation and the use of a host strain deficient in four vacuolar proteinases resulted in α-glucosidase PI expression of about 13% of the soluble protein.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320050104
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