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At least 19 recordsLinked to original sources
PubMed1987

The nucleotide sequence of a streptomycin streptomycin phosphotransferase (streptomycin kinase) [corrected] gene from a streptomycin producer.

The nucleotide sequence of the DNA fragment containing the streptomycin phosphotransferase (streptomycin kinase) [corrected] gene from the streptomycin-producer Streptomyces griseus strain HUT 6037 was determined. Analysis of the sequence revealed an open reading frame which could encode 325 amino acid residues. A biased codon usage pattern, reflecting the high G + C composition (approximately 74%) of Streptomyces DNA, was observed in the gene.

Amino Acid Sequence↗
PubMed1979

Streptomycin sensitivity of ribosomes isolated from a streptomycin-producing Streptomyces griseus.

The streptomycin sensitivity of ribosomes derived from a streptomycin-producing Streptomyces griseus was examined in a polyuridylic acid directed 14C-phenylalanine incorporating system. In order to get reproducible results it is essential to use cell-free extracts which do not inactivate streptomycin. This condition can be fulfilled by the combination of washed ribosomes of the streptomycin-producing strain and the 110 000 g supernatant of the streptomycin-nonproducing variant of S. griseus, because the streptomycin-phosphorylating activity can be washed out from ribosomes of younger streptomycin-producing cultures, and the streptomycin-nonproducing S. griseus does not have any streptomycin-inactivating capacity. In this amino acid polymerizing system the ribosomes of the streptomycin-producing strain were as sensitive to streptomycin as the ribosomes of the nonproducing variant or of Escherichia coli.

Phenylalanine↗
PubMed1977

Effects of membrane-energy mutations and cations on streptomycin and gentamicin accumulation by bacteria: a model for entry of streptomycin and gentamicin in susceptible and resistant bacteria.

Several mutants of Escherichia coli affecting aerobic energy generation and energization of the bacterial membrane have been examined for their effect on streptomycin and gentamicin accumulation and susceptibility. A heme-deficient mutant (K207) and two mutants (CJ-8 [colicin K insensitive] and NR-70) associated with defective aerobic active transport were associated with decreased transport of streptomycin and gentamicin and increased resistance to those antibiotics. These mutants also exhibited increased resistance to several other aminoglycoside antibiotics, but not the aminocyclitol spectinomycin. The same observations were made with a ubiquinone-deficient mutant, but a strA derivative of this mutant was shown additionally to be saturable for streptomycin accumulation at a concentration four or more times lower than that required for saturation of the parent. A mutant uncoupled for adenosine 5'-triphosphate synthesis from electron transport and membrane Mg-adenosine 5'-triphosphatase deficient was hypersensitive to those aminoglycosides tested and spectinomycin, and showed enhanced transport of streptomycin and gentamicin. A variety of compounds structurally related to streptomycin were examined at high concentrations for inhibition of streptomycin uptake in a strA mutant of E. coli K-12 SA 1306, but no evidence for competition was detected, suggesting the absence of a common transport carrier. Four different divalent cations were shown to inhibit streptomycin and gentamicin accumulation in E. coli K-12 SA 1306. Divalent cations were shown to inhibit uptake of these two drugs in two bacterial species with distinct cell wall structures, Pseudomonas aeruginosa and Staphylococcus aureus, and to inhibit streptomycin uptake in spheroplasts of streptomycin-susceptible and -resistant E. coli. However, calcium had almost no inhibitory effect on streptomycin uptake by the ubiquinone-deficient mutant E. coli AN66. These and previous findings have been used to formulate a model for aminoglycoside entry into bacteria using a low-affinity membranous complex involved in membrane energization that includes respiratory quinones, which probably act to bind and transport aminoglycosides across the cell membrane. This phase of transport is associated with the lowest accumulation rate (termed energy-dependent phase I) that is rate limiting for susceptibility. It is further proposed that subsequent association of the membrane-bound aminoglycoside with higher-affinity binding sites on membrane-associated ribosomes carrying out a normal ribosomal cycle and protein synthesis results in a more rapid transport rate (termed energy-dependent phase II). The increased rate could result from a state of membrane energization analogous to that causing enhanced aminoglycoside transport rates seen in the uncoupled mutant, AN120. How this model explains the mechanism by which enzymatically modified aminoglycosides render cells resistant to unmodified aminoglycosides is also discussed.

Adenosine Triphosphatases↗
PubMed1985

Self-cloning in Streptomyces griseus of an str gene cluster for streptomycin biosynthesis and streptomycin resistance.

An str gene cluster containing at least four genes (strR, strA, strB, and strC) involved in streptomycin biosynthesis or streptomycin resistance or both was self-cloned in Streptomyces griseus by using plasmid pOA154. The strA gene was verified to encode streptomycin 6-phosphotransferase, a streptomycin resistance factor in S. griseus, by examining the gene product expressed in Escherichia coli. The other three genes were determined by complementation tests with streptomycin-nonproducing mutants whose biochemical lesions were clearly identified. strR complemented streptomycin-sensitive mutant SM196 which exhibited impaired activity of both streptomycin 6-phosphotransferase and amidinotransferase (one of the streptomycin biosynthetic enzymes) due to a regulatory mutation; strB complemented strain SD141, which was specifically deficient in amidinotransferase; and strC complemented strain SD245, which was deficient in linkage between streptidine 6-phosphate and dihydrostreptose. By deletion analysis of plasmids with appropriate restriction endonucleases, the order of the four genes was determined to be strR-strA-strB-strC. Transformation of S. griseus with plasmids carrying both strR and strB genes enhanced amidinotransferase activity in the transformed cells. Based on the gene dosage effect and the biological characteristics of the mutants complemented by strR and strB, it was concluded that strB encodes amidinotransferase and strR encodes a positive effector required for the full expression of strA and strB genes. Furthermore, it was found that amplification of a specific 0.7-kilobase region of the cloned DNA on a plasmid inhibited streptomycin biosynthesis of the transformants. This DNA region might contain a regulatory apparatus that participates in the control of streptomycin biosynthesis.

Amidinotransferases↗
PubMed1985

Molecular cloning and expression in Streptomyces lividans of a streptomycin 6-phosphotransferase gene from a streptomycin-producing microorganism.

The gene encoding streptomycin 6-kinase involved in the self-resistance of the streptomycin-producing Streptomyces griseus HUT 6037 was cloned in the plasmid vector pIJ703. The resulting plasmid, pSP6, contained 2.5 kb inserts of S. griseus DNA. When streptomycin-susceptible S. lividans 1326 was retransformed with pSP6, all transformants produced streptomycin 6-kinase. Addition of streptomycin to the culture medium of S. lividans carrying pSP6 plasmid brought about a remarkable increase in streptomycin 6-kinase activity in the cell extracts. It is suggested from the results that the production of streptomycin 6-kinase in streptomycin producer was induced by streptomycin accumulated during cultivation.

Cloning, Molecular↗
PubMed1990

[Cross-resistance relationship between streptomycin and kanamycin resistances in Mycobacterium smegmatis (strain Jucho)--comparison of the development patterns of resistances to streptomycin and kanamycin among Mycobacterium tuberculosis, Mycobacterium avium complex, and Mycobacterium smegmatis].

The resistance development pattern of Mycobacterium smegmatis strain 17023 (Jucho) to streptomycin and kanamycin was studied. The medium used was Ogawa egg medium, and the level of resistance was determined for each clone derived from single colony by the 'actual count' method. Hence, the resistance level was estimated as the highest concentration of drugs, in which small inocula consisting of 20 to 100 colony-forming units could grow after seven days incubation. Only one type of resistance mutants resistant to more than 1,000 micrograms/ml streptomycin was isolated and these mutants were also resistant to 8 micrograms/ml kanamycin. On the other hand, only one type of kanamycin-resistant mutants resistant to 8 micrograms/ml kanamycin was isolated and these mutants were also resistant to more than 1,000 micrograms/ml streptomycin. Accordingly, there was a complete cross-resistance relationship between streptomycin and kanamycin resistances. Therefore, there existed only one phenotype, which is simultaneously resistant to streptomycin and kanamycin. The mutants occurred at a rate of about 2 x 10(-8) per viable bacterial population of the parent strain. Streptomycin-dependent mutants occurred at a rate of about 2 x 10(-9). The number of resistant phenotypes to streptomycin and kanamycin was only one in M. smegmatis, while it was five in M. tuberculosis and 2 or 3 in M. avium complex (Tsukamura, M. and Mizuno, S.: J. Gen. Microbiol. 88: 269-274, 1975; Tsukamura, M.: Kekkaku 62: 445-458, 1987). The simplicity of the resistance system of M. smegmatis suggests that this organism is evolutionally primitive in the world of mycobacteria.

Drug Resistance, Microbial↗
PubMed1979

Streptomycin resistance in a streptomycin-producing microorganism.

Cell-free extracts of Streptomyces bikiniensis contain an adenosine 5'-triphosphate-dependent kinase which inactivates streptomycin (Sm) and dihydrostreptomycin by phosphorylation. The products have been identified as streptomycin 6-phosphate and dihydrostreptomycin 6-phosphate. Activity was not present in logarithmic-phase cells, which were susceptible to 25 mug of Sm per ml. In stationary-phase cells, activity appeared 12 h before detectable Sm in the medium. These cells were resistant to more than 200 mug of Sm per ml. Certain S. bikiniensis isolates selected from cultures treated with acriflavine or ethidium bromide lost the ability to produce Sm and became susceptible to 10 mug of Sm per ml throughout their growth. Cell-free extracts of the dye-treated isolates did not inactivate Sm and lacked streptomycin kinase activity at all stages in development. Ribosomes from resistant cells bound the same amount of [(3)H]dihydrostreptomycin as ribosomes from susceptible cells, and there was no correlation between the uptake of [(3)H]dihydrostreptomycin and resistance. The Sm-inactivating enzyme was identified as streptomycin-6-kinase. These results suggest that phosphorylation by streptomycin-6-kinase is a major factor in resistance in S. bikiniensis.

Drug Resistance, Microbial↗
PubMed1975

Ribosomal proteins from streptomycin-resistant and dependent mutants, and revertants from streptomycin-dependence to independence in Bacillus subtilis.

Streptomycin-resistant and dependent mutants were isolated from Bacillus subtilis ATCC 6633. Ribosomal proteins were analysed from six such mutants with chromatography on carboxymethyl cellulose or phosphocellulose columns. An altered specific 30s ribosomal protein, 30B, could be detected in all of these mutants. Streptomycin-independent revertants were isolated from a streptomycin-dependent strain. Some of them had an altered 30s ribosomal protein, 30A, and some others had an altered 30C protein. It was shown that from the data of partial N-terminal amino acid sequences together with amino acid compositions and mobilities on two-dimensional gel electrophoresis of these proteins that 30A, 30B, and 30C proteins were homologous with S5, S12 and S4 of E. coli 30s ribosomal proteins, respectively.

Amino Acid Sequence↗
PubMed1975

Analysis of ribosomal proteins in streptomycin resistant and dependent mutants isolated from streptomycin independent Escherichia coli strains.

Mutants resistant to (Str-R) or dependent on streptomycin (Str-D) were isolated from several streptomycin independent (Str-I) strains of Escherichia coli. From 90 of these mutants ribosomes were isolated and the ribosomal proteins analyzed by two-dimensional polyacrylamide gel electrophoresis. The results which are summarized in Tables 1-4 led to the following conclusions: a) The phenotype (Str-R) or Str-D) of the mutants isolated from the Str-I strains strongly depends on the parental strain. b) No other ribosomal proteins than S4, S5 and S12 seem to be altered by mutations leading to dependence on, independence from or resistance to streptomycin. c) The S4 proteins of the analyzed mutants belong to three groups. The ratio between the groups depends more on the origin of the mutants than on their phenotype. d)Eight new types of altered S4 proteins were detected. It is very likely that many, if not all, of the altered S4 proteins originated by frame shift mutations. e) Some of the mutants differ from the wild type by alterations in three ribosomal proteins (S4, S5 and S12). The alteration in one protein, S4, apparently compensates for that in another protein, S5, in such a way that the original phenotype is expressed. These mutants are therefore an excellent tool for studies at the molecular level on the interaction of ribosomal components within the particle.

Drug Resistance, Microbial↗
PubMed1979

Biosynthesis of streptomycin. Enzymic oxidation of dihydrostreptomycin (6-phosphate) to streptomycin (6-phosphate) with a particulate fraction of Streptomyces griseus.

Resting cells and to a greater extent permeabilized cells of Streptomyces griseus can oxidize dihydrostreptomycin to streptomycin. The dihydrostreptomycin oxidoreductase activity was localized in the 100,000 X g particulate fraction. Sucrose density gradient centrifugation of the particulate suspension gave a band at a density of 1.09 which consisted mainly of membrane vesicles. This fraction had high dihydrostreptomycin oxidoreductase activity. S. griseus protoplasts also contain high oxidoreductase activity. These data are consistent with localization of the enzyme in the cell membrane. Dihydrostreptomycin and dihydrostreptomycin 6-phosphate can both serve as substrates for the oxidoreducatase, but the phosphate was the better substrate in the cell free system. Addition of cofactors was not required for the bound dihydrostreptomycin oxidoreductase. The electron acceptor for the oxidation is unknown. Oxidation of dihydrostreptomycin 6-phosphate to streptomycin 6-phosphate very probably represents the penultimate step in the biosynthesis of streptomycin.

Centrifugation, Density Gradient↗
PubMed1977

Correlation between streptomycin resistance and symbiotic properties of Rhizobium. I. Conversion of spheroplastizing, effective R. trifolii strain B1 to avirulent rods with changed phage and antibiotic patterns after mutation to high level of streptomycin resistance.

Rhizobium trifolii strain B1, which is infective and fixes nitrogen during symbiosis with clover plants, shows a peculiar property to undergo morphological change during growth, i.e. rods are changing into spheroplast-like forms. Moreover, it failed to grow at 38 degrees. It was found that mutation to high level of streptomycin resistance (above 1000 microgram per/ml) caused loss of this property. Further studies showed that simultaneously with the changes in streptomycin resistance other features of this strain were also changed: infectivity for clover plants, sensitivity to high temperature, phages and antibiotics. Mutation to low level of streptomycin resistance did not change the above mentioned features of the strain B1.

Bacteriophages↗
PubMed1988

Improved expression of streptomycin resistance in plants due to a deletion in the streptomycin phosphotransferase coding sequence.

Previous studies have shown that a chimeric streptomycin phosphotransferase (SPT) gene can function as a dominant marker for plant cell transformation. The SPT marker previously described by Jones and co-workers has a limited value since it conferred a useful level of resistance only to a fraction (10%) of Nicotiana plumbaginifolia transgenic lines. Expression of resistance was species specific: no such resistant transformants were found in N. tabacum. In this paper we describe an improved SPT construct that utilizes a mutant Tn5 SPT gene. The mutant gene, SPT*, encodes a protein with a two amino acid deletion close to its COOH-terminus. In N. tabacum cell culture the efficiency of transformation with the improved streptomycin resistance marker was comparable to kanamycin resistance. When the chimeric SPT* gene was introduced linked to a kanamycin resistance gene, streptomycin resistance was expressed in most of the transgenic N. tabacum lines.

Chimera↗
PubMed1976

Derivation and properties of Proteus mirabilis systems for high frequency transduction of streptomycin--sulphonamide and streptomycin-sulphonamide--kanamycin resistances.

Properties of two transducing systems with phages capable of high frequency transduction (HFT) of streptomycin and sulphonamide resistance markers of the V group plasmid R905, and of these markers plus the kanamycin resistance marker derived from a previously described HFT phage 5006MHFTak, are described. Transducing particles of the former phage, named 5006MHFTsus, were detected using the replica-plate technique in an ultraviolet-induced lysate of Proteus mirabilis strain PM5006 transduced to streptomycin and sulphonamide resistance by phage 5006M grown on PM5006 carrying R905. Phage 5006MHFTsusk was also detected by the replica-plate technique in ultraviolet-induced lysates of of phage 5006MHFTsus transductants retransduced to ampicillin and kanamycin resistance by phage 5006MHFTak. Both phages were serologically identical to the parent phage 5006M. Ultraviolet-induced lysates transduced their markers to PM5006 at frequencies of about 5 X 10(-2)/plaque-forming unit adsorbed for both the phages. With phage 5006MHFTsusk, this frequency was increased about 10-fold by simultaneous infection of recipients with homologous non-transducing phage, while phage 5006MHFTsus transductions only underwent a twofold increase. Transductants took about 60 min to express complete resistance to 50 mug streptomycin/ml, and resistance to 1600 mug sulphadiazine/ml was complete within 120 min after phage adsorption. Phage 5006MHFTsusk was slightly more resistant to ultraviolet inaction of its transducing potential and reasons are given for the belief that transductants of both phages are heterogenote-like. Both phage lysates were also capable of generalized transduction and, like previously described HFT phages, lysates transduced the leucine marker at increased frequencies. Using previously described extra- and intra-species phages hosts, it was found that the phages could transduce in single infection and were defective in the lysogenic conversion function as well as in a maturation step. Possible modes of formation of the HFT particles are discussed9

Ampicillin↗
PubMed1975

Two-dimensional gel electrophoresis of ribosomal proteins from streptomycin-sensitive and streptomycin-resistant mutants of Chlamydomonas reinhardi.

Ribosomal proteins from three mutant strains of Chlamydomonas reinhardi were analysed and compared by one-dimensional and two-dimensional gel electrophoresis. One mutant was streptomycin-sensitive the other two were streptomycin-resistant, one with a Mendelian the other with a non-Mendelian pattern of inheritance. In the 30-S subunits of chloroplast ribosomes approximately 25 proteins are found and in the 50-S subunits 34 proteins. The 40-S subunits of cytoplasmic ribosomes contain about 31 proteins and the 60-S subunits 44 proteins. The molecular weights of most proteins in all subunits are in the range of 10 000 to 35 000. However, the 60-S subunits contain in addition a protein of molecular weight 50 000 and the 30-S subunits show 6-7 bands of molecular weights from 50 000 to 83 000. The proteins of the cytoplasmic 80-S ribosomes or of their subunits from all three mutants are electrophoretically identical. The proteins of the 70-S organellar ribosomes and both of their subunits show distinct differences between the three strains. Our results indicate that organellar ribosomal proteins are in part controlled by nuclear DNA and in part by organellar DNA.

Chlamydomonas↗
PubMed1988

A second streptomycin resistance gene from Streptomyces griseus codes for streptomycin-3"-phosphotransferase. Relationships between antibiotic and protein kinases.

Two genes, aphE and orf, coding for putative Mr 29,000 and Mr 31,000, proteins respectively, were identified in the nucleotide sequence of a 2.8 kbp DNA segment cloned from Streptomyces griseus N2-3-11. The aphE gene expressed streptomycin (SM) resistance and a SM phosphorylating enzyme in S. lividans strains. The two genes were found to be in opposite direction and seemed to share a common region of transcription termination. The aphE gene shows significant homology to the aph gene, encoding aminoglycoside 3'-phosphotransferase, APH(3'), from the neomycin-producing S. fradiae. The enzymatic specificity of the aphE gene product was identified to be SM 3"-phosphotransferase, APH(3"). The primary structure of the APH(3") protein is closely related to the members of the APH(3') family of enzymes. However, the APH(3") enzyme did not detectably phosphorylate neomycin or kanamycin. There is only low similarity of the protein to the APH(6) group of SM phosphotransferases. An evolutionary relationship between antibiotic and protein kinases is proposed.

Amino Acid Sequence↗
PubMed1989

[Immediate type anaphylaxis of streptomycin allergy elicited by streptomycin polymers].

It has been known that streptomycin (SM) can cause some immediate type anaphylaxis even anaphylactic shock in clinical therapy. The characteristic of the substance that elicits the allergic reaction has not been reported. Using gel filtration and high performance gel permeation chromatography (HPGPC), we have found that some impurities of high molecular weights (HMW) were formed by heating acidic SM solution. The HMW impurities had a colour reaction with citric acid-acetic anhydride reagent and elicited passive cutaneous anaphylaxis (PCA) on guinea pigs sensitized with rabbit anti-SM-BSA serum and general anaphylaxis in guinea pigs immunized by SM-BSA. It is suggested that the impurities, SM polymers (poly-SM) related to some reactions on amino groups of SM, are the allergens of SM allergy.

Animals↗
PubMed1976

[Effect of the prolonged use of streptomycin as well as streptomycin in combination with tubazid on the bioelectrical activity of the brain in experimental tuberculosis].

The effect of streptomycin used alone and in combination with tubazid on the brain electric activity was studied in chronic experiments on rabbits with tuberculosis. The electrocorticographical investigations showed that the antibacterial treatment lowered the spontaneous electric activity and reactive capacity of the cortex. It was evident from a narrow amplitude of the main rythm, coefficient and energy of synchronization on rythmic photostimulation and paroxysmal activity withing the theta range. With the account of the high therapeutic effect of the antibacterial treatment evident from minimum affection of the organs with tuberculosis, the above changes in the electrocorticogrammes should be attributed to the neurotropic effect of the drug and not to tuberculosis intoxication.

Alpha Rhythm↗