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  • 1
    Electronic Resource
    Electronic Resource
    Integration of exogenous DNA into the genome of Azotobacter vinelandii (1989)
    Springer
    Archives of microbiology 152 (1989), S. 437-440 
    Details
    ISSN: 1432-072X
    Keywords: Genetic transformation ; Plasmid ; Recombination ; pBR322 ; Chromosomal integration ; β-Lactamase ; Azotobacter vinelandii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The soil bacterium Azotobacter vinelandii was genetically transformed by chromosomal integration to ampicillin and/or tetracycline resistance using restriction endonuclease-linearized plasmids. Polyacrylamide gel electrophoresis of protein extracts from three independently isolated ampicillin resistant transformants showed the presence of a 28 Kd band which is the approximate size of the ampicillin resistance gene product (i.e., β-lactamase). Moreover, with nitrocefin, a chromogenic cephalosporin, as a substrate, it was shown that all of the ampicillin resistant transformants produced functional β-lactamase. DNA hybridization showed that the chromosomal DNA from transformed cells contained plasmid DNA sequences at discrete sites. Growth experiments indicated that stable A. vinelandii transformants that carry functional integrated DNA were physiologically impaired.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446925
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  • 2
    Electronic Resource
    Electronic Resource
    Development and enhancement of agricultural biotechnology in some countries in Latin America (1991)
    Springer
    World journal of microbiology and biotechnology 7 (1991), S. 164-170 
    Details
    ISSN: 1573-0972
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A number of research institutions and both local and international agencles in Latin America are using biotechnology as part of an effort to enhance agricultural productivity. However, it is very much an open question as to whether all of these various organizations can provide the best means of realizing this goal. Latin American countries vary dramatically in their knowledge base and current use of modern biotechnology. Thus, while some countries lack the ability to develop, or possibly even implement, many aspects of modern biotechnology, others are quite advanced in this regard. This review provides a somewhat selective overview of current research in the area of agricultural biotechnology in Mexico, Costa Rica and Ecuador, with emphasis on how the existing agencies and institutions have responded to the challenge of biotechnology. In addition, general strategies for the development of agricultural biotechnology in these countries are presented and discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00328986
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  • 3
    Electronic Resource
    Electronic Resource
    Partial characterization ofPseudomonas fluorescens subsp.cellulosa endoglucanase activity produced inEscherichia coli (1990)
    Springer
    Journal of industrial microbiology and biotechnology 5 (1990), S. 59-64 
    Details
    ISSN: 1476-5535
    Keywords: Cellulase ; Endoglucanase ; Cellulose ; Pseudomonas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The recombinant plasmid, pPFC4, which carriesPseudomonas fluorescens subsp.cellulosa chromosomal DNA was previously isolated on the basis of its ability to direct the expression of endoglucanase inEscherichia coli. In the present study, some physical and chemical properties of this activity were characterized. The major portion (78.4%) of the endoglucanase activity is found in the periplasmic space ofE. coli. This plasmid-encoded endoglucanase has a pH optimum of approximately 6.0 and a temperature optimum of approximately 50°C. With carboxymethylcellulose-zymograms, after polyacrylamide gel electrophoresis, periplasmic extracts fromE. coli carrying pPFC4 show six distinct bands with endoglucanase activity. The molecular mass of the major endoglucanase band is approximately 29 kDa while the remaining bands with endoglucanase activity range from 48 to 100 kDa. Although the basis of this heterogeneity is not known, the DNA insert of pPFC4 that encodes endoglucanase activity is not large enough to contain six separate genes; hence, the observed array of endoglucanases may result from post-translational modification of one or two primary gene products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01573853
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  • 4
    Electronic Resource
    Electronic Resource
    DNA sequence analysis of endoglucanase genes fromPseudomonas fluorescens subsp.cellulosa andPseudomonas sp. NCIB 8634 (1990)
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 285-289 
    Details
    ISSN: 1476-5535
    Keywords: Cellulase ; Endoglucanase ; Gene sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The DNA of two previously isolated recombinant clones, one fromPseudomonas sp. NCIB 8634 (=Cellvibrio mixtus) (pPC71) and another fromPseudomonas fluorescens subsp.cellulosa (pPFC4) that express endoglucanase activity inE. coli was sequenced. Plasmid pPC71 had three open reading frames, two of which include portions of plasmid pBR322. The third open reading frame occurs entirely within thePseudomonas DNA insert and encodes a protein with a molecular mass of 5845 Da. The DNA insert in pPFC4 was found to contain an open reading frame (PFC-ORF) that encodes a protein of 32189 Da. The major endoglucanase produced inE. coli cells carrying pPFC4 is about 30000 Da [26]. It is concluded that PFC-ORF encodes this endoglucanase. Both ribosome and catabolite gene activator protein binding sites lie upstream from the initiating codon of PFC-ORF. An interesting feature of the PFC-ORF protein is the presence of amino acid motifs Val-Ser-Ser-Ser-Ser and Val-Val-Ser-Ser-Ser-Ser-Ser that occur within a 25 amino acid span.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01575875
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  • 5
    Electronic Resource
    Electronic Resource
    A complete cDNA for adenine phosphoribosyltransferase fromArabidopsis thaliana (1992)
    Springer
    Plant molecular biology 18 (1992), S. 653-662 
    Details
    ISSN: 1573-5028
    Keywords: adenine phosphoribosyltransferase ; Arabidopsis thaliana ; purine metabolism ; selectable marker
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An intact cDNA fromArabidopsis thaliana for adenine phosphoribosyltransferase (APRT) was isolated and sequenced. The cDNA is 729 nucleotides in length and predicts a protein ofM r 27140. The deduced amino acid sequence has been compared with those of other APRTs and shown to be most similar to theEscherichia coli protein. Construction of a molecular tree of the known APRT amino acid sequences indicates theA. thaliana andE. coli APRT sequences form one cluster and the currently available vertebrate and invertebrate sequences form a separate grouping. Since it is possible to select either for or against the expression of APRT, the isolation of this APRT cDNA clone will allow these selection schemes to be used in plant genetic experiments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00020008
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  • 6
    Electronic Resource
    Electronic Resource
    Isolation and partial characterization of siderophore mutants ofAzotobacter vinelandii (1988)
    Springer
    Current microbiology 17 (1988), S. 343-346 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Azotobacter vinelandii was mutagenized with ethyl methanesulfonate, and colonies that did not produce the fluorescent yellow-green pigment that is characteristic of the wild type were selected. All 32 stable nonfluorescent mutants failed to secrete the siderophore azotobactin and were also impaired to some extent in the production of the second majorA. vinelandii siderophore, azotochelin. Mutants also showed differences in their capacity to grow on medium supplemented with either 200 μM bipyridyl or 200 μM Fe (III). In the absence of iron, an 84-kilodalton outer membrane protein, which is a major derepressed component, was missing in some of the mutants. Thus, siderophore production inA. vinelandii appears to be a highly integrated system in which the syntheses of azotobactin and azotochelin are functionally coupled.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01570875
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  • 7
    Electronic Resource
    Electronic Resource
    Effect of transformation ofAzotobacter vinelandii with the low copy number plasmid pRK290 (1989)
    Springer
    Current microbiology 19 (1989), S. 143-146 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We previously observed that whenAzotobacter vinelandii was transformed by different broad-host-range plasmids, normal cellular functions such as growth and siderophore production are impaired. In the present work, whenA. vinelandii was transformed with the low copy number plasmid pRK290, the extent of this metabolic impairment was lessened, as evidenced by increased siderophore production and moderate levels of growth on medium that lacks added iron. It is concluded that the severity of the plasmid-induced metabolic load reflects the relative level of expression of plasmid-encoded proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01568932
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  • 8
    Electronic Resource
    Electronic Resource
    Plant-microbial interaction under gnotobiotic conditions: A scanning electron microscope study (1991)
    Springer
    Current microbiology 23 (1991), S. 111-114 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Inoculation of canola seeds withPseudomonas putida GR12-2 stimulates root elongation under gnotobiotic conditions. Transformation ofP. putida GR12-2 with the broad-host-range plasmid pGSS15 abolishes the enhancement of root elongation. With scanning electron microscopy it was found that both transformed and nontransformedP. putida GR12-2 are capable of binding to canola seed coats. In addition, it was observed that 4 days after the initial inoculation the roots of bothP. putida GR12-2- and GR12-2/pGSS15-treated seedlings were free of adhering bacteria despite the fact that it was subsequently shown that both bacterial strains are capable of binding to roots. Thus, adhesion to roots is not necessary for the initial phase of enhanced root elongation that is induced byP. putida GR12-2 under gnotobiotic conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02092259
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  • 9
    Electronic Resource
    Electronic Resource
    Purification ofPseudomonas fluorescens subsp.cellulosa endoglucanases produced inEscherichia coli (1990)
    Springer
    Current microbiology 20 (1990), S. 339-342 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Both plasmid pPFC4, which contains 10.6 kb, and a derivative of pPFC4—viz., pPFC4-4.6—which contains 4.6 kb ofPseudomonas fluorescens subsp.cellulosa DNA, direct the synthesis of six distinct endoglucanases inEscherichia coli. Two of these enzymes were purified to homogeneity in a single step by means of anion exchange HPLC. One enzyme has a molecular weight of 30.0 ± 1.0 kDa, an isoelectric point of 7.5, and a specific activity of 3470 U of activity/mg of protein, whereas the other has a molecular weight of 38.5 ± 1.0 kDa, an isoelectric point of 6.7, and a specific activity of 18,050 U of activity/mg of protein. On the basis of the amino acid composition, the 38.5 kDa enzyme appears to be a modified version of the 30.0 kDa enzyme. Thus, the multiplicity of endoglucanases produced inE. coli/pPFC4-4.6 cells may be owing to the posttranslational modification of a smaller number of primary translation products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02091916
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