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  • 1
    Electronic Resource
    Electronic Resource
    Molecular mechanisms regulating the production of collagenase and TIMP in U937 cells: Evidence for involvement of delayed transcriptional activation and enhanced mRNA stability (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 4286-4292 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00067a018
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  • 2
    Electronic Resource
    Electronic Resource
    Production of Extracellular Proteins by Bacteria (1976)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 30 (1976), S. 41-62 
    Details
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.mi.30.100176.000353
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  • 3
    Electronic Resource
    Electronic Resource
    The effect of metal ions on the alkaline phosphatase of Rhizobium leguminosarum (1980)
    Springer
    Archives of microbiology 126 (1980), S. 251-256 
    Details
    ISSN: 1432-072X
    Keywords: Rhizobium leguminosarum ; Alkaline phosphatase ; Phosphomonoesterase ; Mg2+, Zn2+-enzyme, K+ activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The alkaline phosphatase (EC 3.1.3.1.) from Rhizobium leguminosarum WU235 has been purified. The enzyme is a non-specific phosphomonoesterase, has a molecular weight of 78,500 and a sub-unit molecular weight of 39,400. Magnesium and zinc ions are implicated in the structure of the enzyme; atomic absorption analysis gave 1.9 g-atoms Mg2+ and 1.9–5.1 g-atoms Zn2+ per mole of enzyme. In addition high concentrations of Mg2+ markedly stimulate the enzyme. The phosphatase is inhibited by Li+ and Na+ and stimulated by K+, Rb+ and Cs+, which suggests that the enzyme is K+ activated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409928
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  • 4
    Electronic Resource
    Electronic Resource
    Aromatic metabolism in Rhizobium trifolii —protocatechuate 3,4-dioxygenase (1984)
    Springer
    Archives of microbiology 138 (1984), S. 187-190 
    Details
    ISSN: 1432-072X
    Keywords: Rhizobium ; Aromatic metabolism in protocatechuate 3,4-dioxygenase ; R. trifolii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protocatechuate 3,4-dioxygenase (EC 1.13.11.3) has been purified 42-fold from 4-hydroxybenzoate-grown cells of Rhizobium trifolii TA1, where it constitutes about 2% of the cell protein. The dioxygenase has a molecular weight of 220,000, with two dissimilar sub-units of molecular weights 29,000 and 26,500, corresponding to an α4β4 composition. The enzyme is specific for protocatechuate, with a Km of 1.75×10-5 M and maximum activity at pH 9.2. Metal removal and replacement studies indicate that the enzyme contains complexed Fe3+ which is required for activity. Direct atomic absorption analysis gave 1.3–1.5 g atoms Fe3+ per mole of isolated enzyme, but correction for metal-deficient proteins suggests that the value is close to 2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00402117
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  • 5
    Electronic Resource
    Electronic Resource
    4-aminobutyrate is not available to bacteroids of cowpea Rhizobium MNF2030 in snake bean nodules (1990)
    Springer
    Archives of microbiology 153 (1990), S. 455-462 
    Details
    ISSN: 1432-072X
    Keywords: GABA metabolism ; GABA transport ; Cowpea Rhizobium sp ; Bacteroid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Laboratory cultures of cowpea Rhizobium MNF2030 grew on 4-aminobutyrate (GABA) as sole source of carbon and nitrogen. GABA transport was active since it was inhibited by carbonyl cyanide mchlorophenyl hydrazone and 2,4-dinitrophenol and cells developed a 400-fold concentration gradient across the cell membrane. Arsenite treatment of GABA-grown cells revealed stoichiometric conversion of GABA to pyruvate, indicating that 2-oxoglutarate is not an intermediate in GABA catabolism. GABA catabolism by cells of strain MNF2030 grown on GABA appreared to involve GABA transaminase, succinic semialdehyde dehydrogenase and malic enzyme; the first two enzymes were specifically induced by growth on GABA. The deamination process and removal of NH3 in cells catabolizing GABA involved GABA: 2-oxoglutarate transaminase; glutamate: oxaloacetate aminotransferase; asparate: pyruvate aminotransferase and alanine dehydrogenase. Isolated snakebean bacteroids of strain MNF2030 transported only small amounts of GABA and had uninduced levels of GABA catabolic enzymes, even though the nodules contained significant levels of GABA. The data suggest that GABA is not available to snakebean nodule bacteroids, presumably because of a control imposed by the peribacteroid membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248427
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  • 6
    Electronic Resource
    Electronic Resource
    Carbon catabolism in continuous cultures and bacteroids of Rhizobium leguminosarum MNF 3841 (1989)
    Springer
    Archives of microbiology 152 (1989), S. 606-610 
    Details
    ISSN: 1432-072X
    Keywords: Rhizobium leguminosarum ; Catabolic enzymes ; Bacteroids ; Percoll gradients ; Chemostats ; Substrate consumption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Bacteroids of R. leguminosarum MNF3841 isolated from pea nodules using Percoll gradients had activities of TCA cycle enzymes up to 6-fold higher than those measured in free-living cells grown on fumarate or sucrose. Activities of sugar catabolic enzymes on the other hand were 2–14-fold lower in isolated bacteroids than in sucrose-grown free-living cells. In continuous culture, cells of strain MNF3841 grown on sucrose under P i limitation had 2–3-fold higher activities of invertase, glucose-6-phosphate dehydrogenase, the Entner-Doudoroff enzymes and 6-phosphogluconate dehydrogenase, than cells grown on fumarate. With one exception O2 limited cultures had similar activities of the carbon catabolic enzymes to P i-limited cultures grown in the same substrate. Glucose-6-phosphate dehydrogenase in O2-limited cells grown of fumarate was 50% lower than in P i-limited cells. Co-utilization of fumarate and sucrose occurred with chemostat cultures supplied with both under a variety of conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425495
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  • 7
    Electronic Resource
    Electronic Resource
    Selenite uptake and incorporation by Selenomonas ruminatium (1984)
    Springer
    Archives of microbiology 140 (1984), S. 252-256 
    Details
    ISSN: 1432-072X
    Keywords: Selenomonas ruminantium ; Selenite uptake ; Metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Selenite uptake and incorporation in Selenomonas ruminantium was constitutive with an inducible component. It was distinct from sulphate or selenate transport, since sulphate and selenate did not inhbit uptake, nor could sulphate or selenate uptake be demonstrated. Selenite uptake had an apparent K m of 1.28 mM and a V max of 148 ng Se min-1 mg-1 protein. Uptake was sensitive to inhibition by 2,4-dinitrophenol (DNP), carbonyl cyanide m-chlorophenyl hydrazone (CCCP), azide, iodoacetic acid (IAA) and N-ethylmaleimide (NEM), but not chloropromazine (CPZ), N,N′-dicyclohexyl-carbodiimide (DCCD), quinine, arsenate, or fluoride. Treatment of cells accumulating 75[Se]-Selenite with 2,4,DNP inhibited uptake, but did not cause efflux. Transport of selenite was inhibited by sulphite and nitrite, but not by nitrate, phosphate, sulphate of selenate. 75[Se]-Selenite was incorporated into selenocystine, selenoethionine, selenohomocysteine, and selenomethionine and was also reduced to red elemental selenium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00454937
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  • 8
    Electronic Resource
    Electronic Resource
    Ammonium uptake by cowpea Rhizobium strain MNF 2030 and Rhizobium trifolii MNF 1001 (1988)
    Springer
    Archives of microbiology 149 (1988), S. 308-311 
    Details
    ISSN: 1432-072X
    Keywords: Ammonium transport ; Ammonium permease ; Rhizobium trifolii ; Cowpea Rhizobium sp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Free-living Rhizobium trifolii MNF 1001 and cowpea Rhizobium MNF 2030 grown in chemostat culture under nitrogen limitation had high activities of an ammonium permease. In phosphate-limited, nitrogen-excess conditions, strains MNF 1001 and MNF 2030 retained 20% and 50%, respectively, of the ammonium uptake activity found in nitrogen-limited cells. Uptake in both strains was sensitive to azide, cyanide, carbonyl cyanide m-chlorophenyl hydrazone and 2,4-dinitrophenol. A gradient of ammonium concentration greater than 150-fold developed across the membrane within 20 min in cells of strain MNF 1001 grown under ammonia limitation. The pH optimum for ammonium uptake by N-limited cells of both MNF 1001 and MNF 2030 was around pH 7. The apparent K m values for the ammonium permease in strains MNF 2030 and MNF 1001 were 3.9±1.6 μM and 2.0±1.6 μM respectively, and the V max was 47±2.6 nmol min-1 (mg protein)-1 for MNF 2030 and 101±5.1 nmol min-1 (mg protein)-1 for MNF 1001. Isolated snake bean bacteroids of strain MNF 2030 capable of transporting succinate and l-glutamate had no detectable ammonium uptake activity. It therefore appears that the ammonium permeases in cells of these two strains are not as tightly regulated as in R. leguminosarum MNF 3841.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00411647
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  • 9
    Electronic Resource
    Electronic Resource
    Symbiotic and competitive properties of motility mutants of Rhizobium trifolii TA1 (1987)
    Springer
    Archives of microbiology 148 (1987), S. 34-39 
    Details
    ISSN: 1432-072X
    Keywords: Rhizobium trifolii ; Motility mutants ; Nodulating competitiveness ; Nodulaton ; Rhizosphere
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Non-motile mutants of Rhizobium trifolii defective in either flagellar synthesis or function were isolated by transposon Tn5 mutagenesis. they were indistinguishable from motile control strains in growth in both laboratory media and in the rhizosphere of clover roots. When each non-motile mutant was grown together with a motile strain in continuous culture, the numbers of motile and non-motile organisms remained in constant proportion, implying that their growth rates were essentially identical. When inoculated separately onto clover roots, the mutants and wildtype did not differ significantly in the number of nodules produced or in nitrogen fixing activity. However, when mixtures of equal numbers of mutant and wild-type cells were inoculated onto clover roots, the motile strain formed approximately five times more nodules than the flagellate or non-flagellate, non-motile mutants, suggesting that motility is a factor in competition for nodule formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00429644
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  • 10
    Electronic Resource
    Electronic Resource
    Specificity of siderophore-mediated transport of iron in rhizobia (1994)
    Springer
    Archives of microbiology 161 (1994), S. 333-339 
    Details
    ISSN: 1432-072X
    Keywords: Siderophore ; Hydroxamate ; Iron transport ; Rhizobium leguminosarum ; Trihydroxamate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The trihydroxamate siderophore, hydroxamate K, has been purified from culture filtrates of iron-deficient Rhizobium leguminosarum biovar viciae MNF710. The iron complex has a molecular weight of 828 and an absorption maximum at 443 nm (εM=1510). 55Fe complexed to purified hydroxamate K was taken up by MNF710, its hydroxamate-negative mutant MNF7102 and Rhizobium leguminosarum biovar trifolii WU95 via an iron-regulated transport system, but Rhizobium meliloti U45 failed to take up the iron-siderophore complex under any conditions. A similar pattern of iron uptake was observed with ferrioxamine B. MNF710, MNF7102, U45 and WU95 all transported 55Fe-ferrichrome but only the first three strains took up 55Fe-ferrichrome A. All these 55Fe-trihydroxamate uptake systems were ironregulated in MNF710, MNF7102 and WU95. In contrast, uptake of 55Fe-rhodotorulate, a dihydroxamate, was essentially constitutive in all four organisms. Similarly, uptake of 55Fe-citrate and 55Fe-nitrilotriacetic acid was constitutive. None of the strains took up 55Fe complexed with enterobactin or with pyoverdins from Pseudomonas aeruginosa ATCC15692 (PAO1) and Pseudomonas fluorescens ATCC17400.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00303589
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